Proteins are digested in the stomach by pepsin and in the small intestine by trypsin, chymotrypsin, and other enzymes which break proteins down into amino acids. Amino acids are absorbed in the small intestine through active transport systems involving carrier proteins and the glutathione transport system which require energy in the form of ATP. Once inside intestinal cells, amino acids enter the bloodstream and are circulated throughout the body.
Digestive System of the Human Body.
Detailed explaination.
According to ICSE syllabus for grade 9.
This Presentation includes: The alimentary canal, organs and their functions, secretions, processes and definitions.
Based on selina publishers- Biology Part 1 grade 9.
Digestive System of the Human Body.
Detailed explaination.
According to ICSE syllabus for grade 9.
This Presentation includes: The alimentary canal, organs and their functions, secretions, processes and definitions.
Based on selina publishers- Biology Part 1 grade 9.
Introcution to Proteins, Amino Acids and PolypeptidesDHANANJAY PATIL
A comprehensive introduction to the proteins, amino acids and polypeptides. This will give readers a overall view of this topic. All types of queries and suggestions are most welcome
Amino acids have properties that are well-suited to carry out a variety of biological functions
Capacity to polymerize
Useful acid-base properties
Varied physical properties
Varied chemical functionality
In this section, we describe digestion and absorption of proteins.
Most of the slides are cited from:
1. Lippincott's Illustrated Review Biochemistry
2. U. Satyrana Biochemistry
Dr. Haroon
structure of proteins
definition of Digestion
sources of Proteins --> EXOGENEOUS SOURCES 50-100g/day and ENDOGENEOUS SOURCES 30-100g/day
Proteins DEGRADED BY --> HYDROLASES specifically PEPTIDASES(ENDOPEPTIDASES & EXOPEPTIDASES)
1. Gastric Digestion of Proteins
2. Pancreatic Digestion of Proteins
3. Digestion of Proteins by Small Intestine Enzymes
Absorption of Amino ACids by Na+Dependent, Na+ Independent, Meister Cycle or gama-glutamyl cycle
Introcution to Proteins, Amino Acids and PolypeptidesDHANANJAY PATIL
A comprehensive introduction to the proteins, amino acids and polypeptides. This will give readers a overall view of this topic. All types of queries and suggestions are most welcome
Amino acids have properties that are well-suited to carry out a variety of biological functions
Capacity to polymerize
Useful acid-base properties
Varied physical properties
Varied chemical functionality
In this section, we describe digestion and absorption of proteins.
Most of the slides are cited from:
1. Lippincott's Illustrated Review Biochemistry
2. U. Satyrana Biochemistry
Dr. Haroon
structure of proteins
definition of Digestion
sources of Proteins --> EXOGENEOUS SOURCES 50-100g/day and ENDOGENEOUS SOURCES 30-100g/day
Proteins DEGRADED BY --> HYDROLASES specifically PEPTIDASES(ENDOPEPTIDASES & EXOPEPTIDASES)
1. Gastric Digestion of Proteins
2. Pancreatic Digestion of Proteins
3. Digestion of Proteins by Small Intestine Enzymes
Absorption of Amino ACids by Na+Dependent, Na+ Independent, Meister Cycle or gama-glutamyl cycle
Transformation, à l'intérieur de l'appareil digestif, des aliments en substances chimiques de faible poids moléculaire, capables de passer dans la circulation sanguine
Proteins are the most abundant organic molecules of the living system.
They occur in every part of the cell and constitute about 50% of the cellular dry weight.
Proteins form the fundamental basis of structure and function of life.
Amino acids are the monomers that make up proteins
It's a brief article about digestion and metabolism in human body for premedical student .
Taking about digestion a long the GIT system and metabolism of carbohydrates , protein , lipids, and nucleoproteins.
Nucleophilic Addition of carbonyl compounds.pptxSSR02
Nucleophilic addition is the most important reaction of carbonyls. Not just aldehydes and ketones, but also carboxylic acid derivatives in general.
Carbonyls undergo addition reactions with a large range of nucleophiles.
Comparing the relative basicity of the nucleophile and the product is extremely helpful in determining how reversible the addition reaction is. Reactions with Grignards and hydrides are irreversible. Reactions with weak bases like halides and carboxylates generally don’t happen.
Electronic effects (inductive effects, electron donation) have a large impact on reactivity.
Large groups adjacent to the carbonyl will slow the rate of reaction.
Neutral nucleophiles can also add to carbonyls, although their additions are generally slower and more reversible. Acid catalysis is sometimes employed to increase the rate of addition.
hematic appreciation test is a psychological assessment tool used to measure an individual's appreciation and understanding of specific themes or topics. This test helps to evaluate an individual's ability to connect different ideas and concepts within a given theme, as well as their overall comprehension and interpretation skills. The results of the test can provide valuable insights into an individual's cognitive abilities, creativity, and critical thinking skills
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/
BREEDING METHODS FOR DISEASE RESISTANCE.pptxRASHMI M G
Plant breeding for disease resistance is a strategy to reduce crop losses caused by disease. Plants have an innate immune system that allows them to recognize pathogens and provide resistance. However, breeding for long-lasting resistance often involves combining multiple resistance genes
What is greenhouse gasses and how many gasses are there to affect the Earth.moosaasad1975
What are greenhouse gasses how they affect the earth and its environment what is the future of the environment and earth how the weather and the climate effects.
Deep Behavioral Phenotyping in Systems Neuroscience for Functional Atlasing a...Ana Luísa Pinho
Functional Magnetic Resonance Imaging (fMRI) provides means to characterize brain activations in response to behavior. However, cognitive neuroscience has been limited to group-level effects referring to the performance of specific tasks. To obtain the functional profile of elementary cognitive mechanisms, the combination of brain responses to many tasks is required. Yet, to date, both structural atlases and parcellation-based activations do not fully account for cognitive function and still present several limitations. Further, they do not adapt overall to individual characteristics. In this talk, I will give an account of deep-behavioral phenotyping strategies, namely data-driven methods in large task-fMRI datasets, to optimize functional brain-data collection and improve inference of effects-of-interest related to mental processes. Key to this approach is the employment of fast multi-functional paradigms rich on features that can be well parametrized and, consequently, facilitate the creation of psycho-physiological constructs to be modelled with imaging data. Particular emphasis will be given to music stimuli when studying high-order cognitive mechanisms, due to their ecological nature and quality to enable complex behavior compounded by discrete entities. I will also discuss how deep-behavioral phenotyping and individualized models applied to neuroimaging data can better account for the subject-specific organization of domain-general cognitive systems in the human brain. Finally, the accumulation of functional brain signatures brings the possibility to clarify relationships among tasks and create a univocal link between brain systems and mental functions through: (1) the development of ontologies proposing an organization of cognitive processes; and (2) brain-network taxonomies describing functional specialization. To this end, tools to improve commensurability in cognitive science are necessary, such as public repositories, ontology-based platforms and automated meta-analysis tools. I will thus discuss some brain-atlasing resources currently under development, and their applicability in cognitive as well as clinical neuroscience.
The use of Nauplii and metanauplii artemia in aquaculture (brine shrimp).pptxMAGOTI ERNEST
Although Artemia has been known to man for centuries, its use as a food for the culture of larval organisms apparently began only in the 1930s, when several investigators found that it made an excellent food for newly hatched fish larvae (Litvinenko et al., 2023). As aquaculture developed in the 1960s and ‘70s, the use of Artemia also became more widespread, due both to its convenience and to its nutritional value for larval organisms (Arenas-Pardo et al., 2024). The fact that Artemia dormant cysts can be stored for long periods in cans, and then used as an off-the-shelf food requiring only 24 h of incubation makes them the most convenient, least labor-intensive, live food available for aquaculture (Sorgeloos & Roubach, 2021). The nutritional value of Artemia, especially for marine organisms, is not constant, but varies both geographically and temporally. During the last decade, however, both the causes of Artemia nutritional variability and methods to improve poorquality Artemia have been identified (Loufi et al., 2024).
Brine shrimp (Artemia spp.) are used in marine aquaculture worldwide. Annually, more than 2,000 metric tons of dry cysts are used for cultivation of fish, crustacean, and shellfish larva. Brine shrimp are important to aquaculture because newly hatched brine shrimp nauplii (larvae) provide a food source for many fish fry (Mozanzadeh et al., 2021). Culture and harvesting of brine shrimp eggs represents another aspect of the aquaculture industry. Nauplii and metanauplii of Artemia, commonly known as brine shrimp, play a crucial role in aquaculture due to their nutritional value and suitability as live feed for many aquatic species, particularly in larval stages (Sorgeloos & Roubach, 2021).
Comparing Evolved Extractive Text Summary Scores of Bidirectional Encoder Rep...University of Maribor
Slides from:
11th International Conference on Electrical, Electronics and Computer Engineering (IcETRAN), Niš, 3-6 June 2024
Track: Artificial Intelligence
https://www.etran.rs/2024/en/home-english/
DERIVATION OF MODIFIED BERNOULLI EQUATION WITH VISCOUS EFFECTS AND TERMINAL V...Wasswaderrick3
In this book, we use conservation of energy techniques on a fluid element to derive the Modified Bernoulli equation of flow with viscous or friction effects. We derive the general equation of flow/ velocity and then from this we derive the Pouiselle flow equation, the transition flow equation and the turbulent flow equation. In the situations where there are no viscous effects , the equation reduces to the Bernoulli equation. From experimental results, we are able to include other terms in the Bernoulli equation. We also look at cases where pressure gradients exist. We use the Modified Bernoulli equation to derive equations of flow rate for pipes of different cross sectional areas connected together. We also extend our techniques of energy conservation to a sphere falling in a viscous medium under the effect of gravity. We demonstrate Stokes equation of terminal velocity and turbulent flow equation. We look at a way of calculating the time taken for a body to fall in a viscous medium. We also look at the general equation of terminal velocity.
2. Learning Objectives
What are Proteins?
Composition of Proteins.
Digestion of Proteins.
Absorption of Proteins.
Absorption of Amino acids.
3. What are Proteins?
• Proteins are the most abundant
organic molecule of the living
system.
• It forms the fundamental basis of
structure and function of life.
• They are macromolecules.
4. They constitute about 50% of the
cellular dry weight.
They are not only the cell building
blocks; they also execute all the cell
functions.
Proteins are the polymers of amino
acid.
5. Function of Proteins
Protein performs a very great variety of
specialized and essential functions in the
living cells.
These functions may be broadly grouped
as Static (Structural) and Dynamic
functions.
10. In the human digestive system, food
enters the mouth and mechanical
digestion of the food starts by the action of
mastication (chewing), a form of
mechanical digestion, and the wetting
contact of saliva. (Physical Digestion).
11. Digestion in Mouth
There is no digestion of protein in mouth
because no proteolytic enzymes present
in the saliva.
Saliva only lubricate the food, this helps
in making food soluble for the action of
proteolytic enzymes.
13. Digestion in Stomach
Digestion of proteins starts in stomach.
When proteins enters the stomach, it
stimulates the secretion of gastrin
hormone.
This gastrin, in turn, stimulates the release
of gastric juice which contains;
• Hydrochloric acid (HCL).
• Pepsinogen (zymogen).
• Rennin in infants.
pH of gastric juice = 1.5 to 2.5
14. Role of gastric HCL
It causes denaturation of proteins.
It convert proteins to meta proteins
which are easily digested.
It converts pepsinogen to pepsin.
It makes pH in the stomach suitable for
the action of pepsin.
15. Role of Pepsin
It is activated by HCl by auto activation.
Its optimum pH is 1.5-2.2
It is an endo peptidases acting on the
central peptide bond.
It is secreted in active form called
pepsinogen.
Pepsinogen HCl Pepsin.
16. Role of Rennin
It is a milk-clotting enzyme.
It is present in the stomach of infants
and young animals.
Its optimum pH is 4.
It converts casein of milk into
paracasein.
It combines with calcium forming
calcium paracaseinate.
18. Digestion in Pancrease
Trypsin:
• It is an endopeptidases and secreted in
an inactive form called trypsinogen.
• Its optimum pH is 8.
• It is activated by entero-kinases.
• It hydrolyze central peptide bond in
which the carboxylic group belongs to
basic amino acid.
• Trypsinogen enterokinases Trypsin
19. Chymotrypsin
It is the endopeptidase and secreted in
an
inactive form.
Its optimum pH is 8.
It is activated by trypsin.
It hydrolyze the central peptide bond in
which the carboxylic group belongs to
aromatic amino acid.
20. Elastase
It is also endopeptidases and secreted
in an inactive form called proelastase.
Its optimum pH is 8.
It is activated by trypsin.
It digests elastin and collagen.
It hydrolyze the central peptide bond in
which the carboxylic group belongs to
aromatic amino acid.
22. Definintion:
A carboxypetidase is a protease enzyme that
hydrolyzes a peptide bond at the carboxy-
terminal of a protein or peptide.
23. Funtions
The first carboxypeptidases studied were
those involved in the digestion of foods.
e.g. Pancreatic Carboxypeptidases A₁,A₂,
and B.
However, most of the known
carboxypeptidases is not involved in
catabolism; they help to mature protein.
e.g. the biosynthesis of neuroendocrine
peptides such as insulin requires a
carboxypeptidase.
24. Classfication by Substrate
Preference
This classification system for
carboxypeptidases refers to their substrate
preference.
Carboxypeptidase A:
Pancreatic exocarboxypeptidases that
have a stronger preference for those amino
acids containing aromatic or branched
hydrocarbon chains are called
carboxypeptidases A (A for aromatic or
aliphatic).
25.
26. Carboxypeptidase B:
Those carboxypeptidases that cleave
positively charged amino acids are called
carboxypeptidase B (B for basic).
e.g. arginine, lysine
28. Digestion in Intestine
Aminopeptidases:
It is an exopeptidases.
It acts on the terminal peptide bond at
the amino terminal of the peptide chain.
Dipeptidases:
It acts on dipeptide.
It releases two amino acids.
Tripeptidases:
It act on tripeptide.
It releases single amino acid and dipeptide.
29. Absorption of Proteins
It is an active process that needs
energy.
Energy needed is derived from
hydrolysis
From ATP.
This process occurs in small intestine.
Absorption of amino acids is rapid in the
Duodenum and jejunum but slow in the
Ileum.
30. Mechanism of Amino Acids
Absorption
There are two mechanisms of amino acids
absorption.
1. Carrier Protein Transport System.
2. Glutathione Transport System
(Glutamyl Cycle).
32. Carrier Protein Transport
System
It is the main system for amino acid
absorption.
It is an active process that needs
energy.
The energy needed is derived from ATP
molecule.
There are seven carrier proteins, one for
each group of amino acids.
33. Each carrier protein has two sides.
One for amino acid and another one for
sodium.
It co-transport s amino acids and sodium
from intestinal lumem to cytosol of
intestinal mucosa cells.
The absorbed amino acid passes to the
portal circulation, while sodium is
extruded out of the cell with exchange
with potassium (K+) by Sodum (Na+).
35. Glutathione Transport
System
It is also known as Glutamyl Cycle.
Glutathione is used to transport amino
acids from intestinal lumen to cytosol of
intestinal mucosa cells.
It is an active process that needs
energy.
The energy needed is derived from ATP.
Absorption of one amino acid molecule
need 3 ATP.
36. Glutathione reacts with amino acid in the
presence of glutacyl.
Glutamyl amino acid releases amino
acid in the cytosol of intestinal mucosa
cell with formation of 5-oxoproline that is
used for regeneration of glutathione to
begin another turn of the cycle.
37. Oxoprolinuria:
It is a disease caused by a defect in
glutathione synthetase enzyme.
It is characterised by accumulation of
5-oxoproline in blood and hence
excreted in urine.
It is associated with mental
retardation.
39. Absorption of Intact Proteins
and polypeptides
This period is short period, immediately
after birth.
The small intestine of infants can absorb
intact prroteins and polypeptide by
endocytosis or pioncytosis.
40. Intact proteins and polypeptides are not
absorbed by the adult intestine.
Macromolecular absorption in certain
individuals appears to be responsible for
antibody formation that often causes
food allergy.
41. Absorption of Amino
Acids
The absorption occurs mainly in the
small intestine.
It is an energy requiring process.
The di- and tripeptidases, after being
absorbed are hydrolyzed into free amino
acids in the cytosol of epithilial cells.
The activities of dipeptidases are high in
these cells.
42. L-Amino acids are more rapidly
absorbed than D-amino acids.
The transport of L-amino acids occurs
by an active process.
D-amino acids by a simple diffusion.
43. Mechanism of absorption of
amino acids
Na+ dependant active process and
requires ATP.
Na+ diffuses along the concentration
gradient. The amino acid also enters
the intestinal cell.
Na+ and amino acids share a common
carrier and transported together.
The compound ‘cytochlasin’ inhibits Na+
independent transport system.