This document summarizes the digestion and absorption of proteins. It explains that proteins are broken down into amino acids by proteolytic enzymes in the stomach, pancreas, and small intestine. These amino acids are then absorbed into the bloodstream through active transport mechanisms in the intestinal epithelium. Genetic disorders like Hartnup's disease and cystinuria can impair amino acid transport and cause amino acids to be lost in urine or feces.
This document summarizes protein digestion, absorption, and excretion in the human body. It describes how proteins are broken down mechanically and chemically in the mouth, stomach and small intestine through the actions of enzymes. The end products of digestion - amino acids, dipeptides and tripeptides - are then absorbed in the small intestine through active transport and carrier proteins. Most absorbed amino acids are transported to the liver, where they are used for protein synthesis, generating glucose or urea, which is excreted in urine. Some diseases can impact protein digestion and absorption if enzymes are damaged or transport processes are impaired.
The document summarizes the digestion and absorption of amino acids. It describes how proteins are broken down into peptides and individual amino acids by proteolytic enzymes in the stomach, pancreas, and intestines. The amino acids are then absorbed into the bloodstream through active transport mechanisms in the small intestine and transported via the portal vein to other tissues. Deficiencies in enzymes involved in amino acid metabolism or transport can cause clinical issues.
This document summarizes amino acid metabolism and nitrogen balance in the human body. It discusses how proteins are the main source of nitrogen and how nitrogen balance is determined by comparing nitrogen intake from dietary proteins and nitrogen loss from waste products. It describes the conditions of positive, negative and neutral nitrogen balance. It also outlines the processes of protein digestion and absorption in the stomach and small intestine, as well as the major pathways for amino acid degradation, including deamination, transamination, and decarboxylation.
The document summarizes protein digestion and absorption in the gastrointestinal tract. It discusses how proteins are broken down into peptides and amino acids via enzymes in the stomach and small intestine. Pepsin begins protein digestion in the stomach, while trypsin, chymotrypsin, and peptidases further break peptides into amino acids in the small intestine. Amino acids and di/tripeptides are then absorbed across the intestinal epithelium via transporters and released into the bloodstream. Some diseases that impact protein absorption, like Hartnup disease and cystinuria, are also mentioned.
This document summarizes the digestion and absorption of proteins in the human body. It discusses that proteins are obtained endogenously from digestive enzymes and cells, as well as exogenously from dietary intake. The stomach contains hydrochloric acid and pepsin to denature and break down proteins. The pancreas secretes trypsinogen, chymotrypsinogen, and other zymogens which are activated and further digest proteins into peptides and amino acids in the small intestine. Aminopeptidases and dipeptidases on intestinal cells complete the digestion. Amino acids are then absorbed via active transport systems involving sodium and ATP. Deficiencies or defects in these digestive processes can impair protein digestion.
This document summarizes the digestion and absorption of proteins. It explains that proteins are broken down into amino acids by proteolytic enzymes in the stomach, pancreas, and small intestine. These amino acids are then absorbed into the bloodstream through active transport mechanisms in the intestinal epithelium. Genetic disorders like Hartnup's disease and cystinuria can impair amino acid transport and cause amino acids to be lost in urine or feces.
This document summarizes protein digestion, absorption, and excretion in the human body. It describes how proteins are broken down mechanically and chemically in the mouth, stomach and small intestine through the actions of enzymes. The end products of digestion - amino acids, dipeptides and tripeptides - are then absorbed in the small intestine through active transport and carrier proteins. Most absorbed amino acids are transported to the liver, where they are used for protein synthesis, generating glucose or urea, which is excreted in urine. Some diseases can impact protein digestion and absorption if enzymes are damaged or transport processes are impaired.
The document summarizes the digestion and absorption of amino acids. It describes how proteins are broken down into peptides and individual amino acids by proteolytic enzymes in the stomach, pancreas, and intestines. The amino acids are then absorbed into the bloodstream through active transport mechanisms in the small intestine and transported via the portal vein to other tissues. Deficiencies in enzymes involved in amino acid metabolism or transport can cause clinical issues.
This document summarizes amino acid metabolism and nitrogen balance in the human body. It discusses how proteins are the main source of nitrogen and how nitrogen balance is determined by comparing nitrogen intake from dietary proteins and nitrogen loss from waste products. It describes the conditions of positive, negative and neutral nitrogen balance. It also outlines the processes of protein digestion and absorption in the stomach and small intestine, as well as the major pathways for amino acid degradation, including deamination, transamination, and decarboxylation.
The document summarizes protein digestion and absorption in the gastrointestinal tract. It discusses how proteins are broken down into peptides and amino acids via enzymes in the stomach and small intestine. Pepsin begins protein digestion in the stomach, while trypsin, chymotrypsin, and peptidases further break peptides into amino acids in the small intestine. Amino acids and di/tripeptides are then absorbed across the intestinal epithelium via transporters and released into the bloodstream. Some diseases that impact protein absorption, like Hartnup disease and cystinuria, are also mentioned.
This document summarizes the digestion and absorption of proteins in the human body. It discusses that proteins are obtained endogenously from digestive enzymes and cells, as well as exogenously from dietary intake. The stomach contains hydrochloric acid and pepsin to denature and break down proteins. The pancreas secretes trypsinogen, chymotrypsinogen, and other zymogens which are activated and further digest proteins into peptides and amino acids in the small intestine. Aminopeptidases and dipeptidases on intestinal cells complete the digestion. Amino acids are then absorbed via active transport systems involving sodium and ATP. Deficiencies or defects in these digestive processes can impair protein digestion.
The document summarizes the key processes of digestion and absorption in the gastrointestinal tract. It discusses:
1) The three main stages of digestion - mechanical and chemical breakdown of food, secretion of enzymes and electrolytes to provide optimal conditions for digestion, and transport of nutrients into the bloodstream.
2) The major secretions at each stage - saliva, gastric juices, pancreatic and bile secretions, and secretions from the small intestine.
3) The enzymes and constituents involved in digesting carbohydrates, proteins, lipids, and their absorption mechanisms.
4) Some common digestive disorders that can result from enzyme deficiencies or malabsorption.
Transformation, à l'intérieur de l'appareil digestif, des aliments en substances chimiques de faible poids moléculaire, capables de passer dans la circulation sanguine
The human digestive system consists of two major component one is the accessory organ like liver pancreas gall bladder salivary gland and other is the Alimentary canal which is started from oral cavity and ends on anal cavity.
in this ppt all parts are described briefly for better understanding.
1) Dietary proteins are digested into smaller peptides and individual amino acids through the action of proteolytic enzymes in the stomach, pancreas, and small intestine.
2) Key digestive enzymes include pepsin in the stomach and trypsin, chymotrypsin, and carboxypeptidases in the pancreas.
3) Amino acids are then absorbed into the bloodstream across the intestinal mucosa through active transport mechanisms involving sodium-dependent and independent carriers.
Digestion and absorption of proteins for Medical SchoolRavi Kiran
This document summarizes the digestion and absorption of proteins in the human body. It discusses:
1) The proteolytic enzymes that break down proteins into peptides and amino acids in the stomach and small intestine, such as pepsin, trypsin, and chymotrypsin.
2) The categories of proteases (protein-digesting enzymes) including exopeptidases, endopeptidases, and their examples.
3) The absorption of amino acids in the small intestine and their transport to various organs in the body like the brain, kidneys, and liver.
4) The intracellular breakdown of proteins by cathepsins, the ubiquitin pathway, and proteasomes.
5 digestion absorption of carbs,proteins,lipids.pptxAnnaKhurshid
The document summarizes digestion and absorption of carbohydrates, proteins, and lipids. It describes:
- Carbohydrate digestion begins in the mouth and continues in the stomach and small intestine where pancreatic enzymes break down starches and sugars into monosaccharides like glucose that are then absorbed.
- Protein digestion begins when pepsin breaks down proteins in the stomach. Further digestion occurs via pancreatic proteases like trypsin in the small intestine, resulting in amino acid absorption.
- Lipid digestion is initiated in the stomach but occurs mainly via pancreatic lipase in the small intestine after bile emulsifies lipids into smaller droplets for enzyme access. Free fatty acids and monoacylglycerols are produced and absorbed.
This document discusses gastric secretions and their regulation. The stomach secretes acid, water, electrolytes, and enzymes to aid in digestion. Acid secretion is controlled by hormones like gastrin and histamine which stimulate acid production, and somatostatin which inhibits it. The stomach has oxyntic glands in the body/fundus containing parietal cells that secrete acid, and pyloric glands in the antrum containing G cells that secrete gastrin. H. pylori infection can disrupt this balance and cause ulcers or cancer if chronic.
This document summarizes renal handling of various substances including glucose, proteins, amino acids, organic acids, cations, anions, and uric acid. It describes that glucose and amino acids are freely filtered by the kidneys and nearly completely reabsorbed in the proximal tubule via secondary active transport. Proteins and peptides are also reabsorbed, with peptides being degraded into amino acids. Organic acids and cations may be filtered and secreted from the blood into the urine via active transport mechanisms in the proximal tubule. Uric acid is produced from purine metabolism and is primarily excreted by the kidneys within normal limits to avoid precipitation and gout.
protein metabolism
https://www.facebook.com/pages/%D8%A7%D9%84%D8%B9%D9%84%D8%A7%D8%AC-%D8%A7%D9%84%D9%85%D8%B5%D8%B1%D9%8A-%D9%84%D9%81%D9%8A%D8%B1%D9%88%D8%B3-%D8%B3%D9%89-%D9%88%D8%A7%D9%84%D8%A7%D9%8A%D8%AF%D8%B2/239710159549535
The document summarizes digestion and absorption in non-ruminants. It describes how carbohydrates are broken down into monosaccharides in the small intestine through enzymes like amylase and absorbed into the bloodstream. Proteins are broken into oligopeptides and amino acids by stomach and pancreatic enzymes and absorbed across the intestinal wall. Lipids are emulsified and broken into fatty acids and glycerol by pancreatic lipase in the small intestine and absorbed via chylomicrons. Vitamins and minerals are also absorbed in the small intestine through various mechanisms.
Proteins are polymers made of amino acids linked by peptide bonds. There are 20 standard amino acids, some of which are essential to obtain from diet as the body cannot synthesize them. Amino acids are classified based on essentiality and presence of functional groups. Proteins are digested into amino acids in the stomach by pepsin and further in the small intestine by pancreatic enzymes like trypsin. Amino acids and small peptides are absorbed into the bloodstream and transported to tissues where they are used for growth, repair, energy and synthesis of other proteins and molecules. Excess amino acids are converted to urea which is excreted in urine.
The document discusses protein and amino acid metabolism. It covers:
1. The digestion of proteins into amino acids in the stomach and small intestine by enzymes like pepsin and trypsin.
2. The 20 standard amino acids and their classification as essential/non-essential and glucogenic/ketogenic.
3. The transport of amino acids in blood to cells and their role in protein synthesis and degradation via ubiquitination and proteasomes.
The document summarizes the digestion and absorption of proteins in the human body. Dietary and endogenous proteins are broken down through digestion by enzymes in the stomach, pancreas, and intestines. In the stomach, pepsin digests proteins into proteoses and peptones. The pancreas secretes trypsin, chymotrypsin, and other enzymes as zymogens which are activated and further break down proteins. In the intestines, aminopeptidases and dipeptidases break down peptides into amino acids, which are then absorbed into the bloodstream through active transport mechanisms.
The document provides an overview of hepatic physiology. It discusses the anatomy and blood supply of the liver, physiologic immaturity of hepatic function in newborns, mechanisms of hepatic regeneration, hepatic protein and carbohydrate metabolism, bilirubin uptake and metabolism, and pathways of hepatic drug metabolism. Key points include the segmental anatomy of the liver, extramedullary hematopoiesis in the fetal liver, factors involved in hepatic regeneration, major proteins synthesized by the liver, and the role of conjugation in bilirubin excretion.
Nutrition micro nutrient that determined Proteinsamuelmerga3
This document discusses proteins and amino acids. It defines proteins as molecules composed of amino acids that are necessary for life. There are essential amino acids that must be obtained from food, and nonessential amino acids that the body can produce. The roles of proteins include being building blocks, enzymes, hormones, and parts of antibodies. Proteins are broken down into amino acids during digestion and reassembled during protein synthesis.
This document provides information on vitamins, including their definition, types, and details on specific water-soluble and fat-soluble vitamins. It discusses the structure, absorption, functions, requirements, sources, and deficiencies of several B vitamins including thiamine, riboflavin, niacin, pyridoxine, pantothenic acid, and their roles in biochemical processes in the body.
The document summarizes the multi-step process of protein digestion and absorption in the human body. Proteins are broken down into smaller peptides and amino acids via proteolytic enzymes in the stomach and pancreas. Amino acids and small peptides are then absorbed into the bloodstream via active transport mechanisms in the small intestine. The liver plays an important role in receiving absorbed amino acids and converting excess nitrogen into urea for excretion.
1) Nitrogen enters the body through dietary protein and is metabolized through amino acids. Amino acids are broken down and the nitrogen is removed as ammonia, which is converted to urea to be excreted.
2) The amino acid pool and protein turnover are key concepts in nitrogen metabolism. Amino acids from protein breakdown replenish the amino acid pool, which is also used for protein synthesis and other processes.
3) Dietary proteins are digested by enzymes in the stomach and pancreas into dipeptides and tripeptides, then fully into amino acids by intestinal enzymes for absorption.
describes the sources of lipids. enzymes and stages of digestion in detail. absorption form , transport form and disorders of digestion & absorption included.
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...AbdullaAlAsif1
The pygmy halfbeak Dermogenys colletei, is known for its viviparous nature, this presents an intriguing case of relatively low fecundity, raising questions about potential compensatory reproductive strategies employed by this species. Our study delves into the examination of fecundity and the Gonadosomatic Index (GSI) in the Pygmy Halfbeak, D. colletei (Meisner, 2001), an intriguing viviparous fish indigenous to Sarawak, Borneo. We hypothesize that the Pygmy halfbeak, D. colletei, may exhibit unique reproductive adaptations to offset its low fecundity, thus enhancing its survival and fitness. To address this, we conducted a comprehensive study utilizing 28 mature female specimens of D. colletei, carefully measuring fecundity and GSI to shed light on the reproductive adaptations of this species. Our findings reveal that D. colletei indeed exhibits low fecundity, with a mean of 16.76 ± 2.01, and a mean GSI of 12.83 ± 1.27, providing crucial insights into the reproductive mechanisms at play in this species. These results underscore the existence of unique reproductive strategies in D. colletei, enabling its adaptation and persistence in Borneo's diverse aquatic ecosystems, and call for further ecological research to elucidate these mechanisms. This study lends to a better understanding of viviparous fish in Borneo and contributes to the broader field of aquatic ecology, enhancing our knowledge of species adaptations to unique ecological challenges.
Immersive Learning That Works: Research Grounding and Paths ForwardLeonel Morgado
We will metaverse into the essence of immersive learning, into its three dimensions and conceptual models. This approach encompasses elements from teaching methodologies to social involvement, through organizational concerns and technologies. Challenging the perception of learning as knowledge transfer, we introduce a 'Uses, Practices & Strategies' model operationalized by the 'Immersive Learning Brain' and ‘Immersion Cube’ frameworks. This approach offers a comprehensive guide through the intricacies of immersive educational experiences and spotlighting research frontiers, along the immersion dimensions of system, narrative, and agency. Our discourse extends to stakeholders beyond the academic sphere, addressing the interests of technologists, instructional designers, and policymakers. We span various contexts, from formal education to organizational transformation to the new horizon of an AI-pervasive society. This keynote aims to unite the iLRN community in a collaborative journey towards a future where immersive learning research and practice coalesce, paving the way for innovative educational research and practice landscapes.
The document summarizes the key processes of digestion and absorption in the gastrointestinal tract. It discusses:
1) The three main stages of digestion - mechanical and chemical breakdown of food, secretion of enzymes and electrolytes to provide optimal conditions for digestion, and transport of nutrients into the bloodstream.
2) The major secretions at each stage - saliva, gastric juices, pancreatic and bile secretions, and secretions from the small intestine.
3) The enzymes and constituents involved in digesting carbohydrates, proteins, lipids, and their absorption mechanisms.
4) Some common digestive disorders that can result from enzyme deficiencies or malabsorption.
Transformation, à l'intérieur de l'appareil digestif, des aliments en substances chimiques de faible poids moléculaire, capables de passer dans la circulation sanguine
The human digestive system consists of two major component one is the accessory organ like liver pancreas gall bladder salivary gland and other is the Alimentary canal which is started from oral cavity and ends on anal cavity.
in this ppt all parts are described briefly for better understanding.
1) Dietary proteins are digested into smaller peptides and individual amino acids through the action of proteolytic enzymes in the stomach, pancreas, and small intestine.
2) Key digestive enzymes include pepsin in the stomach and trypsin, chymotrypsin, and carboxypeptidases in the pancreas.
3) Amino acids are then absorbed into the bloodstream across the intestinal mucosa through active transport mechanisms involving sodium-dependent and independent carriers.
Digestion and absorption of proteins for Medical SchoolRavi Kiran
This document summarizes the digestion and absorption of proteins in the human body. It discusses:
1) The proteolytic enzymes that break down proteins into peptides and amino acids in the stomach and small intestine, such as pepsin, trypsin, and chymotrypsin.
2) The categories of proteases (protein-digesting enzymes) including exopeptidases, endopeptidases, and their examples.
3) The absorption of amino acids in the small intestine and their transport to various organs in the body like the brain, kidneys, and liver.
4) The intracellular breakdown of proteins by cathepsins, the ubiquitin pathway, and proteasomes.
5 digestion absorption of carbs,proteins,lipids.pptxAnnaKhurshid
The document summarizes digestion and absorption of carbohydrates, proteins, and lipids. It describes:
- Carbohydrate digestion begins in the mouth and continues in the stomach and small intestine where pancreatic enzymes break down starches and sugars into monosaccharides like glucose that are then absorbed.
- Protein digestion begins when pepsin breaks down proteins in the stomach. Further digestion occurs via pancreatic proteases like trypsin in the small intestine, resulting in amino acid absorption.
- Lipid digestion is initiated in the stomach but occurs mainly via pancreatic lipase in the small intestine after bile emulsifies lipids into smaller droplets for enzyme access. Free fatty acids and monoacylglycerols are produced and absorbed.
This document discusses gastric secretions and their regulation. The stomach secretes acid, water, electrolytes, and enzymes to aid in digestion. Acid secretion is controlled by hormones like gastrin and histamine which stimulate acid production, and somatostatin which inhibits it. The stomach has oxyntic glands in the body/fundus containing parietal cells that secrete acid, and pyloric glands in the antrum containing G cells that secrete gastrin. H. pylori infection can disrupt this balance and cause ulcers or cancer if chronic.
This document summarizes renal handling of various substances including glucose, proteins, amino acids, organic acids, cations, anions, and uric acid. It describes that glucose and amino acids are freely filtered by the kidneys and nearly completely reabsorbed in the proximal tubule via secondary active transport. Proteins and peptides are also reabsorbed, with peptides being degraded into amino acids. Organic acids and cations may be filtered and secreted from the blood into the urine via active transport mechanisms in the proximal tubule. Uric acid is produced from purine metabolism and is primarily excreted by the kidneys within normal limits to avoid precipitation and gout.
protein metabolism
https://www.facebook.com/pages/%D8%A7%D9%84%D8%B9%D9%84%D8%A7%D8%AC-%D8%A7%D9%84%D9%85%D8%B5%D8%B1%D9%8A-%D9%84%D9%81%D9%8A%D8%B1%D9%88%D8%B3-%D8%B3%D9%89-%D9%88%D8%A7%D9%84%D8%A7%D9%8A%D8%AF%D8%B2/239710159549535
The document summarizes digestion and absorption in non-ruminants. It describes how carbohydrates are broken down into monosaccharides in the small intestine through enzymes like amylase and absorbed into the bloodstream. Proteins are broken into oligopeptides and amino acids by stomach and pancreatic enzymes and absorbed across the intestinal wall. Lipids are emulsified and broken into fatty acids and glycerol by pancreatic lipase in the small intestine and absorbed via chylomicrons. Vitamins and minerals are also absorbed in the small intestine through various mechanisms.
Proteins are polymers made of amino acids linked by peptide bonds. There are 20 standard amino acids, some of which are essential to obtain from diet as the body cannot synthesize them. Amino acids are classified based on essentiality and presence of functional groups. Proteins are digested into amino acids in the stomach by pepsin and further in the small intestine by pancreatic enzymes like trypsin. Amino acids and small peptides are absorbed into the bloodstream and transported to tissues where they are used for growth, repair, energy and synthesis of other proteins and molecules. Excess amino acids are converted to urea which is excreted in urine.
The document discusses protein and amino acid metabolism. It covers:
1. The digestion of proteins into amino acids in the stomach and small intestine by enzymes like pepsin and trypsin.
2. The 20 standard amino acids and their classification as essential/non-essential and glucogenic/ketogenic.
3. The transport of amino acids in blood to cells and their role in protein synthesis and degradation via ubiquitination and proteasomes.
The document summarizes the digestion and absorption of proteins in the human body. Dietary and endogenous proteins are broken down through digestion by enzymes in the stomach, pancreas, and intestines. In the stomach, pepsin digests proteins into proteoses and peptones. The pancreas secretes trypsin, chymotrypsin, and other enzymes as zymogens which are activated and further break down proteins. In the intestines, aminopeptidases and dipeptidases break down peptides into amino acids, which are then absorbed into the bloodstream through active transport mechanisms.
The document provides an overview of hepatic physiology. It discusses the anatomy and blood supply of the liver, physiologic immaturity of hepatic function in newborns, mechanisms of hepatic regeneration, hepatic protein and carbohydrate metabolism, bilirubin uptake and metabolism, and pathways of hepatic drug metabolism. Key points include the segmental anatomy of the liver, extramedullary hematopoiesis in the fetal liver, factors involved in hepatic regeneration, major proteins synthesized by the liver, and the role of conjugation in bilirubin excretion.
Nutrition micro nutrient that determined Proteinsamuelmerga3
This document discusses proteins and amino acids. It defines proteins as molecules composed of amino acids that are necessary for life. There are essential amino acids that must be obtained from food, and nonessential amino acids that the body can produce. The roles of proteins include being building blocks, enzymes, hormones, and parts of antibodies. Proteins are broken down into amino acids during digestion and reassembled during protein synthesis.
This document provides information on vitamins, including their definition, types, and details on specific water-soluble and fat-soluble vitamins. It discusses the structure, absorption, functions, requirements, sources, and deficiencies of several B vitamins including thiamine, riboflavin, niacin, pyridoxine, pantothenic acid, and their roles in biochemical processes in the body.
The document summarizes the multi-step process of protein digestion and absorption in the human body. Proteins are broken down into smaller peptides and amino acids via proteolytic enzymes in the stomach and pancreas. Amino acids and small peptides are then absorbed into the bloodstream via active transport mechanisms in the small intestine. The liver plays an important role in receiving absorbed amino acids and converting excess nitrogen into urea for excretion.
1) Nitrogen enters the body through dietary protein and is metabolized through amino acids. Amino acids are broken down and the nitrogen is removed as ammonia, which is converted to urea to be excreted.
2) The amino acid pool and protein turnover are key concepts in nitrogen metabolism. Amino acids from protein breakdown replenish the amino acid pool, which is also used for protein synthesis and other processes.
3) Dietary proteins are digested by enzymes in the stomach and pancreas into dipeptides and tripeptides, then fully into amino acids by intestinal enzymes for absorption.
describes the sources of lipids. enzymes and stages of digestion in detail. absorption form , transport form and disorders of digestion & absorption included.
Unlocking the mysteries of reproduction: Exploring fecundity and gonadosomati...AbdullaAlAsif1
The pygmy halfbeak Dermogenys colletei, is known for its viviparous nature, this presents an intriguing case of relatively low fecundity, raising questions about potential compensatory reproductive strategies employed by this species. Our study delves into the examination of fecundity and the Gonadosomatic Index (GSI) in the Pygmy Halfbeak, D. colletei (Meisner, 2001), an intriguing viviparous fish indigenous to Sarawak, Borneo. We hypothesize that the Pygmy halfbeak, D. colletei, may exhibit unique reproductive adaptations to offset its low fecundity, thus enhancing its survival and fitness. To address this, we conducted a comprehensive study utilizing 28 mature female specimens of D. colletei, carefully measuring fecundity and GSI to shed light on the reproductive adaptations of this species. Our findings reveal that D. colletei indeed exhibits low fecundity, with a mean of 16.76 ± 2.01, and a mean GSI of 12.83 ± 1.27, providing crucial insights into the reproductive mechanisms at play in this species. These results underscore the existence of unique reproductive strategies in D. colletei, enabling its adaptation and persistence in Borneo's diverse aquatic ecosystems, and call for further ecological research to elucidate these mechanisms. This study lends to a better understanding of viviparous fish in Borneo and contributes to the broader field of aquatic ecology, enhancing our knowledge of species adaptations to unique ecological challenges.
Immersive Learning That Works: Research Grounding and Paths ForwardLeonel Morgado
We will metaverse into the essence of immersive learning, into its three dimensions and conceptual models. This approach encompasses elements from teaching methodologies to social involvement, through organizational concerns and technologies. Challenging the perception of learning as knowledge transfer, we introduce a 'Uses, Practices & Strategies' model operationalized by the 'Immersive Learning Brain' and ‘Immersion Cube’ frameworks. This approach offers a comprehensive guide through the intricacies of immersive educational experiences and spotlighting research frontiers, along the immersion dimensions of system, narrative, and agency. Our discourse extends to stakeholders beyond the academic sphere, addressing the interests of technologists, instructional designers, and policymakers. We span various contexts, from formal education to organizational transformation to the new horizon of an AI-pervasive society. This keynote aims to unite the iLRN community in a collaborative journey towards a future where immersive learning research and practice coalesce, paving the way for innovative educational research and practice landscapes.
The ability to recreate computational results with minimal effort and actionable metrics provides a solid foundation for scientific research and software development. When people can replicate an analysis at the touch of a button using open-source software, open data, and methods to assess and compare proposals, it significantly eases verification of results, engagement with a diverse range of contributors, and progress. However, we have yet to fully achieve this; there are still many sociotechnical frictions.
Inspired by David Donoho's vision, this talk aims to revisit the three crucial pillars of frictionless reproducibility (data sharing, code sharing, and competitive challenges) with the perspective of deep software variability.
Our observation is that multiple layers — hardware, operating systems, third-party libraries, software versions, input data, compile-time options, and parameters — are subject to variability that exacerbates frictions but is also essential for achieving robust, generalizable results and fostering innovation. I will first review the literature, providing evidence of how the complex variability interactions across these layers affect qualitative and quantitative software properties, thereby complicating the reproduction and replication of scientific studies in various fields.
I will then present some software engineering and AI techniques that can support the strategic exploration of variability spaces. These include the use of abstractions and models (e.g., feature models), sampling strategies (e.g., uniform, random), cost-effective measurements (e.g., incremental build of software configurations), and dimensionality reduction methods (e.g., transfer learning, feature selection, software debloating).
I will finally argue that deep variability is both the problem and solution of frictionless reproducibility, calling the software science community to develop new methods and tools to manage variability and foster reproducibility in software systems.
Exposé invité Journées Nationales du GDR GPL 2024
Current Ms word generated power point presentation covers major details about the micronuclei test. It's significance and assays to conduct it. It is used to detect the micronuclei formation inside the cells of nearly every multicellular organism. It's formation takes place during chromosomal sepration at metaphase.
ESPP presentation to EU Waste Water Network, 4th June 2024 “EU policies driving nutrient removal and recycling
and the revised UWWTD (Urban Waste Water Treatment Directive)”
Travis Hills' Endeavors in Minnesota: Fostering Environmental and Economic Pr...Travis Hills MN
Travis Hills of Minnesota developed a method to convert waste into high-value dry fertilizer, significantly enriching soil quality. By providing farmers with a valuable resource derived from waste, Travis Hills helps enhance farm profitability while promoting environmental stewardship. Travis Hills' sustainable practices lead to cost savings and increased revenue for farmers by improving resource efficiency and reducing waste.
The debris of the ‘last major merger’ is dynamically youngSérgio Sacani
The Milky Way’s (MW) inner stellar halo contains an [Fe/H]-rich component with highly eccentric orbits, often referred to as the
‘last major merger.’ Hypotheses for the origin of this component include Gaia-Sausage/Enceladus (GSE), where the progenitor
collided with the MW proto-disc 8–11 Gyr ago, and the Virgo Radial Merger (VRM), where the progenitor collided with the
MW disc within the last 3 Gyr. These two scenarios make different predictions about observable structure in local phase space,
because the morphology of debris depends on how long it has had to phase mix. The recently identified phase-space folds in Gaia
DR3 have positive caustic velocities, making them fundamentally different than the phase-mixed chevrons found in simulations
at late times. Roughly 20 per cent of the stars in the prograde local stellar halo are associated with the observed caustics. Based
on a simple phase-mixing model, the observed number of caustics are consistent with a merger that occurred 1–2 Gyr ago.
We also compare the observed phase-space distribution to FIRE-2 Latte simulations of GSE-like mergers, using a quantitative
measurement of phase mixing (2D causticality). The observed local phase-space distribution best matches the simulated data
1–2 Gyr after collision, and certainly not later than 3 Gyr. This is further evidence that the progenitor of the ‘last major merger’
did not collide with the MW proto-disc at early times, as is thought for the GSE, but instead collided with the MW disc within
the last few Gyr, consistent with the body of work surrounding the VRM.
When I was asked to give a companion lecture in support of ‘The Philosophy of Science’ (https://shorturl.at/4pUXz) I decided not to walk through the detail of the many methodologies in order of use. Instead, I chose to employ a long standing, and ongoing, scientific development as an exemplar. And so, I chose the ever evolving story of Thermodynamics as a scientific investigation at its best.
Conducted over a period of >200 years, Thermodynamics R&D, and application, benefitted from the highest levels of professionalism, collaboration, and technical thoroughness. New layers of application, methodology, and practice were made possible by the progressive advance of technology. In turn, this has seen measurement and modelling accuracy continually improved at a micro and macro level.
Perhaps most importantly, Thermodynamics rapidly became a primary tool in the advance of applied science/engineering/technology, spanning micro-tech, to aerospace and cosmology. I can think of no better a story to illustrate the breadth of scientific methodologies and applications at their best.
Remote Sensing and Computational, Evolutionary, Supercomputing, and Intellige...University of Maribor
Slides from talk:
Aleš Zamuda: Remote Sensing and Computational, Evolutionary, Supercomputing, and Intelligent Systems.
11th International Conference on Electrical, Electronics and Computer Engineering (IcETRAN), Niš, 3-6 June 2024
Inter-Society Networking Panel GRSS/MTT-S/CIS Panel Session: Promoting Connection and Cooperation
https://www.etran.rs/2024/en/home-english/
1. Protein Digestion and Absorption
Christine Waasdorp Hurtado, MD, MSCS, FAAP
Gregg Kobak, MD
University of Colorado School of Medicine
Children’s Hospital Colorado
Reviewed by:
Michael Narkewicz, MD
Jeremiah Levine, MD
2. NASPGHAN
Physiology Education Series
Series Editors:
Christine Waasdorp Hurtado, MD, MSCS, FAAP
Christine.Waasdorp@childrenscolorado.org
Daniel Kamin, MD
Daniel.Kamin@childrens.harvard.edu
3. Protein Digestion Objectives
• Understand the structure of protein
• Understand protein digestion and absorption
• Discuss clinical implications
4. What is Protein?
• Proteins are sequences of amino acids
• There are 20 amino acids
– 9 are essential amino acids
• phenylalanine, valine, threonine, tryptophan, isoleucine,
methionine, histidine, leucine, lysine
– 11 are non-essential
– 4 amino acids are considered conditionally essential
• arginine, tyrosine, glutamine, and cysteine (glycine, proline and
serine sometimes considered conditionally essential)
• Require 0.75g/kg body weight
– Increased requirements in infants and illness
5. Amino Acids: Structure
• Consist of a central carbon
atom bonded to: a hydrogen,
a carboxylic acid, an amino
group, and an additional side
group that is unique to each
amino acid
• The side group creates
unique characteristics for
each amino acid so they
differ in: shape, size,
composition, electrical
charge, and pH
H
H N
H
C
R
C OH
O
Amino
Group
Side
Group
Carboxyl
Group
6. • Amino acids (AA) are linked to form proteins
• Amino acids are joined by PEPTIDE bonds
– Dipeptide – 2 amino acids
– Tripeptide – 3 amino acids
– Oligopeptides – 4-10 amino acids
– Polypeptide – more than 10 amino acids
• Most proteins in the body and diet are long
polypeptides (100s of AA)
Amino Acids: Structure
8. Protein Digestion
• Whole proteins are not absorbed
– Too large to pass through intact cell membranes
• They must be digested into di- and tri-peptides or
individual AAs prior to absorption
– Additional digestion occurs in the cytosol
• Structures of protein are more diverse than
carbohydrates
– Require broad spectrum peptidases and transporters
9. Protein Digestion - Mouth
• No digestion occurs in the oral cavity or esophagus
10. Protein Digestion - Stomach
• Gastric phase
– Gastrin released from G
cells
• Stretch receptors stimulate
release
• AA in stomach stimulate release
– Parietal cells secrete HCl
• Gastrin stimulates Parietal cells to
secrete HCl
• HCl denatures proteins - 40, 30,
and 20 structures
• Converts pepsinogen to pepsin
Image from: Sweety Mehta
11. Protein Digestion - Stomach
– Chief cells secrete Pepsinogen
• Stimulated by cephalic vagal input
• Secretion enhanced
– Acetylcholine, CCK and gastrin
– Pepsinogen is auto-activated at pH <4 to Pepsin
– Cleavage of an N-terminal peptide
– Pepsin can break down collagen
– Pepsin cleaves proteins at large aliphatic or aromatic side
groups
• Completes ~ 10-20% of digestion
– Pepsin is inactivated at pH >4.5
– Protects intestinal tissues
– Protein leaves stomach as mix of insoluble protein, soluble
protein, peptides and amino acids
12. Protein Digestion - Intestines
• Intestinal phase
Overview
– Majority of proteolysis
occurs in the intestines
• 70% of proteins are converted
to oligopeptides
– Still require terminal
action at enterocyte
membrane
Image from: Sweety Mehta
13. Protein Digestion – Small Intestine
• Majority of protein digestion occurs within the
intestine due to the action of pancreatic proteases.
– Proteases break down polypeptides into smaller peptides
and AA
• Two main forms of pancreatic enzymes
– Endopeptidase – cleaves internal bonds
– Ectopeptidase – cleaves AA at C-terminus
15. Pancreatic Proteases
• Pancreatic enzymes stored in acinar cells as pro-enzymes
(zymogens)
– Trypsinogen Trypsin
– Chymotrypsinogen Chymotrypsin
– Procarboxypeptidase A and B Carboxypeptidase A and B
– Proelastase Elastase
16. Protein Digestion - Pancreas
• Zymogens are converted to active form in the intestine
– Trypsinogen Trypsin
• Endopeptidase
– Cleaves on carbonyl side of Lysine & Arginine
– Chymotrypsinogen Chymotrypsin
• Endopeptidase
– Cleaves carboxy terminal tyrosine, phenylalanine, tryptophan, methionine, and
leucine
– Procarboxypeptidase A/B Carboxypeptidase
• Ectopeptidase
– Removes carboxy terminal residues
Enterokinase/ Trypsin
Trypsin
Trypsin
17. • Large peptides from gastric proteolysis are sequentially
cleaved in the small intestine
– Endopeptidases – cleave in the middle of peptide chains
• Trypsin
• Chymotrypsin
• Elastase
– Yield shorter chains with neutral or basic AA at C-terminus
– Carboxypeptidase A and Carboxypeptidase B then act
• Carboxypeptidase A act on neutral AA
• Carboxypeptidase B acts on basic AA
Protein Digestion - Intestine
18. Protein Digestion - Trypsin Inhibitors
• Small proteins or peptides
• Present in plants, organs, and fluids
– Soybeans, peas, beans, wheat
– Pancreas, colostrum
• Decrease activity of trypsin
– Decrease all other proteases activated by trypsin
• Inactivated by heat
19. Protein Digestion - Mucosal
• Intraluminal degradation of proteins by gastric and
pancreatic enzymes is incomplete
• Brush border hydrolysis necessary
• Diversity of substrates requires diverse hydrolyases
• Membrane bound on villi
• Not present in crypt cells
• Produce free AA and small peptides
20. Protein Digestion - Mucosal
Small intestine
(brush border)
– Aminopeptidases
• Cleave at N-terminal AA
– Dipeptidases
• Cleave dipeptides
– Carboxypeptidases
• Cleaves at the carboxy-
terminal
Image from John Yaw-Jong Tsai
21. Protein Digestion - Cytosol
• The vast majority of di- and tri-peptides are digested
into amino acids by cytoplasmic peptidases.
• Peptidases
– Cleave N-terminal AAs
22. Protein Absorption Overview
• Most protein absorption takes place in the
duodenum and jejunum
– Tripeptides, Dipeptides and AA are absorbed
– There is minimal absorption of peptides longer than
three amino acids
• Most AA are absorbed into the bloodstream, but
some remain in the enterocytes and are used to
support the cells
• >99% of protein enters the bloodstream as amino
acids
23. Protein Absorption - Peptides
• Essentially no absorption of peptides
longer than three amino acids
• Di- and tri-peptides are more rapidly
absorbed than free amino acids due
to PEPT1
– Active transporter – PEPT1
• Coupled to sodium-hydrogen exchanger
(NHE3)
• Accommodates various sizes and charges
• Di- and tri-peptides are digested into
amino acids by cytoplasmic
peptidases
Groff & Gropper, 2000
PEPT1
NHE3
25. Protein Absorption - Amino Acids
• The Na+ dependent transporters mechanism
– Transporter binds amino acids only after binding sodium
– Conformational change occurs - dumping Na+ and the
amino acid into the cytoplasm
– The transporter then re-orients back to its original form
allow transport of the next amino acid
– Absorption of amino acids is dependent on the
electrochemical gradient of Na+ across the epithelium
26. Protein Absorption - Amino Acids
• There are 7 transporters of free amino acids in the
brush border
• Mechanism varies
–Na+-independent carriers (2)
• Proton co-transport
• Facilitated diffusion
–Na+-dependent (5)
• Carriers are coupled to Na+ concentration
gradient
27. Protein Transport - Enterocyte
• The basolateral
membrane of the
enterocyte contains
transporters which
export amino acids from
the cell into the blood
– Diffusion
– Both Na+ dependent and
independent carriers
• Only free amino acids
absorbed into blood
Groff & Gropper, 2000
28. Protein Absorption - Intact Proteins
• Absorption of intact proteins occurs rarely
• Shortly after birth, neonates can absorb intact
proteins
• Very few proteins can get through the gauntlet of
soluble (lumen) and membrane-bound proteases
intact
• “Normal” enterocytes do not have the transporters
needed to carry proteins across the plasma membrane
and they can’t permeate tight junctions
29. Clinical Correlation
• Hartnup Disease
– Abnormal transport of neutral AA (ie – tryptophan)
• Mutation in SCL6A19 transporter
– Clinical variability
• No symptoms to rash or neurologic symptoms
• Due to lack of nicotinamide (tryptophan metabolite)
– Diagnosis
• High levels of neutral AA in the urine
– Treatment – supplement with nicotinamide
30. Clinical Correlation
• Cystinuria
– Decreased intestinal absorption of dibasic AA (lysine, arginine,
cystine)
• Defect in SLC3A1 transporter
– Presentation
• Kidney stones – accounts for 10%
– Diagnosis
• Elevated urine cystine
– Treatment
• Hydration
• Limit dietary sodium and methionine
31. Protein Digestion - Summary
• Proteins are digested into amino acids and di and tri
peptides in the stomach and small intestine
– The vast majority of digestion is due to pancreatic enzymes
• Enterokinase plays a key role in pancreatic enzyme activation
– A small percentage of digestion occurs following absorption
into the cytosol
• Absorption is complex
– Several different transporters
– Several different mechanisms
33. Review Question
• The intestinal phase is responsible for the bulk of
protein digestion. What enzymes are active in the
intestines?
– HCL and Pepsinogen
– Endopeptidase and Ectopeptidase
– Pepsin and Trypsin
– Trypsin, Chymotrypsin and Proelastase