This document discusses immunoglobulins (antibodies) and their structure. It notes that antibodies are Y-shaped proteins produced by plasma cells to neutralize pathogens. Each antibody has two identical antigen-binding sites and consists of two light chains and two heavy chains joined by disulfide bonds. The variable regions at the ends of the Y arms form the antigen-binding site, while the constant stems and lower arms form the Fc region which interacts with immune cells and complement proteins.
BP-605T, Pharmaceutical biotechnology, Structure of immunoglobulins, classification of immunoglobulins, explanation of structure of immunoglobulin, digestion with proteolytic enzymes, Fab region, Fc region, role of different immunoglobulin classes, structure of IGM, IGA, IGG, IGE, IGD, Light chain, heavy chain, kappa, lambda, papain enzyme, pepsin enzyme
Antigen-antibody interaction, or antigen-antibody reaction, is a specific chemical interaction between antibodies produced by B cells of the white blood cells and antigens during immune reaction. ... The specificity of the binding is due to specific chemical constitution of each antibody
This topic covers the brief introduction of Ag and Ab in detail. Types and functions of Ig is explained in detail. Paraproteinemias is explained with simple pictures.
by Dr. N.Sivaranjani, MD
BP-605T, Pharmaceutical biotechnology, Structure of immunoglobulins, classification of immunoglobulins, explanation of structure of immunoglobulin, digestion with proteolytic enzymes, Fab region, Fc region, role of different immunoglobulin classes, structure of IGM, IGA, IGG, IGE, IGD, Light chain, heavy chain, kappa, lambda, papain enzyme, pepsin enzyme
Antigen-antibody interaction, or antigen-antibody reaction, is a specific chemical interaction between antibodies produced by B cells of the white blood cells and antigens during immune reaction. ... The specificity of the binding is due to specific chemical constitution of each antibody
This topic covers the brief introduction of Ag and Ab in detail. Types and functions of Ig is explained in detail. Paraproteinemias is explained with simple pictures.
by Dr. N.Sivaranjani, MD
Antibodies are immune system-related proteins called immunoglobulins. Each antibody consists of four polypeptides– two heavy chains and two light chains joined to form a "Y" shaped molecule. ... This variable region, composed of 110-130 amino acids, give the antibody its specificity for binding antigen.
ANTIGEN, HAPTEN, ALL TYPES OF ANTIGENS, IMMUNOGEN , ATTRIBUTES OF ANTIGENICITY, DETERMINANTS OF ANTIGENICITY,
IMMUNOLOGY KUBY, MEDICAL MICROBIOLOGY & IMMUNOLOGY OF PANIKER , LIPPINCOTT'S IMMUNOLOGY, OTHER SOURCES.
antibodies are a large proteins. based on electrophorosis and centrifugation anti bodies are mainly five types .these are protects on human body from various microorganisms.
I took major content from this website i came across. https://www.thevirtualnotebook.com
it's legit since it's sources are books. My other references are mentioned in the last second clip.
Antibodies are immune system-related proteins called immunoglobulins. Each antibody consists of four polypeptides– two heavy chains and two light chains joined to form a "Y" shaped molecule. ... This variable region, composed of 110-130 amino acids, give the antibody its specificity for binding antigen.
ANTIGEN, HAPTEN, ALL TYPES OF ANTIGENS, IMMUNOGEN , ATTRIBUTES OF ANTIGENICITY, DETERMINANTS OF ANTIGENICITY,
IMMUNOLOGY KUBY, MEDICAL MICROBIOLOGY & IMMUNOLOGY OF PANIKER , LIPPINCOTT'S IMMUNOLOGY, OTHER SOURCES.
antibodies are a large proteins. based on electrophorosis and centrifugation anti bodies are mainly five types .these are protects on human body from various microorganisms.
I took major content from this website i came across. https://www.thevirtualnotebook.com
it's legit since it's sources are books. My other references are mentioned in the last second clip.
Immunoglobulins:
The Antibodies or Immunoglobulins are globular proteins present in the serum and tissue fluids. They are produced by the plasma cells (B-cells) and are used in the immune system of the body to neutralize pathogenic microbes or other toxic foreign components.
IgG is the most commonly
discussed antibody molecule,
it is one of the five immunoglobulin
isotypes.https://www.creative-biolabs.com/resource/pdf/com/infographic/A-Brief-Introduction-to-Antibodies-Creative-Biolabs.pdf
Hybridoma technology is a technology of forming hybrid cell lines (hybridomas) by fusing a specific antibody-producing B cell with a myeloma (B cell cancer) cell that is selected for its ability to grow in tissue culture and for an absence of antibody chain synthesis. The antibodies produced by the hybridoma are all of a single specificity and are therefore monoclonal antibodies.https://www.creative-biolabs.com/custom-antibody-development.html
What is an Antibody?Immunoglobulins: Classes and Sub classesvarinder kumar
Forms
History
Immunoglobulins: Classes and Sub classes
Epitope
Antibodies structure
Antibody–antigen interactions
Function
Medical Applications
Regulations
Preclinical studies
Structure prediction
Antibody mimetic
Structure and function of immunoglobulins(antibodies) Likhith KLIKHITHK1
Immunoglobulins (Ig) or antibodies are glycoproteins that are produced by plasma cells. B cells are instructed by specific immunogens.For, example, bacterial proteins, to differentiate into plasma cells, which are protein-making cells that participate in humoral immune responses against bacteria, viruses, fungi, parasites, cellular antigens, chemicals, and synthetic substances.
The immunogen or antigen reacts with a B-cell receptor (BCR) on the cell surface of B lymphocytes, and a signal is produced that directs the activation of transcription factors to stimulate the synthesis of antibodies, which are highly specific for the immunogen that stimulated the B cell. Furthermore, one clone of B cell makes an immunoglobulin (specificity). Besides, the immune system remembers the antigens that caused a previous reaction (memory) due to the development of memory B cells. These are intermediate, differentiated B cells with the capability to quickly become plasma cells. Circulating antibodies recognize antigen in tissue fluids and serum. This activity describes the physiology and pathophysiology of immunoglobulins
Antibody, Y shaped protein complex belonging to immunoglobulin (Ig) superfamily, exists in many kinds of organisms, especially higher animals. Specific antibody can bind specifically to particular exogenous pathogen like virus or bacteria to either directly neutralize the pathogens by blocking its active sites or facilitate the elimination of pathogens by other immune cells, such as macrophages. Antibody is produced by B lymphocytes (plasma cells). B cells initially express antibodies on the cell membrane as B cell receptors (BCR). When BCRs are coupled with desired pathogens, B cells are differentiated into plasma cells, producing a myriad of antibodies. Part of plasma cells transform into memory cells which respond relatively fast to the same substance upon later infection. https://www.creative-biolabs.com/antibody-antigen-faq.htm
THE IMPORTANCE OF MARTIAN ATMOSPHERE SAMPLE RETURN.Sérgio Sacani
The return of a sample of near-surface atmosphere from Mars would facilitate answers to several first-order science questions surrounding the formation and evolution of the planet. One of the important aspects of terrestrial planet formation in general is the role that primary atmospheres played in influencing the chemistry and structure of the planets and their antecedents. Studies of the martian atmosphere can be used to investigate the role of a primary atmosphere in its history. Atmosphere samples would also inform our understanding of the near-surface chemistry of the planet, and ultimately the prospects for life. High-precision isotopic analyses of constituent gases are needed to address these questions, requiring that the analyses are made on returned samples rather than in situ.
Seminar of U.V. Spectroscopy by SAMIR PANDASAMIR PANDA
Spectroscopy is a branch of science dealing the study of interaction of electromagnetic radiation with matter.
Ultraviolet-visible spectroscopy refers to absorption spectroscopy or reflect spectroscopy in the UV-VIS spectral region.
Ultraviolet-visible spectroscopy is an analytical method that can measure the amount of light received by the analyte.
Richard's aventures in two entangled wonderlandsRichard Gill
Since the loophole-free Bell experiments of 2020 and the Nobel prizes in physics of 2022, critics of Bell's work have retreated to the fortress of super-determinism. Now, super-determinism is a derogatory word - it just means "determinism". Palmer, Hance and Hossenfelder argue that quantum mechanics and determinism are not incompatible, using a sophisticated mathematical construction based on a subtle thinning of allowed states and measurements in quantum mechanics, such that what is left appears to make Bell's argument fail, without altering the empirical predictions of quantum mechanics. I think however that it is a smoke screen, and the slogan "lost in math" comes to my mind. I will discuss some other recent disproofs of Bell's theorem using the language of causality based on causal graphs. Causal thinking is also central to law and justice. I will mention surprising connections to my work on serial killer nurse cases, in particular the Dutch case of Lucia de Berk and the current UK case of Lucy Letby.
Observation of Io’s Resurfacing via Plume Deposition Using Ground-based Adapt...Sérgio Sacani
Since volcanic activity was first discovered on Io from Voyager images in 1979, changes
on Io’s surface have been monitored from both spacecraft and ground-based telescopes.
Here, we present the highest spatial resolution images of Io ever obtained from a groundbased telescope. These images, acquired by the SHARK-VIS instrument on the Large
Binocular Telescope, show evidence of a major resurfacing event on Io’s trailing hemisphere. When compared to the most recent spacecraft images, the SHARK-VIS images
show that a plume deposit from a powerful eruption at Pillan Patera has covered part
of the long-lived Pele plume deposit. Although this type of resurfacing event may be common on Io, few have been detected due to the rarity of spacecraft visits and the previously low spatial resolution available from Earth-based telescopes. The SHARK-VIS instrument ushers in a new era of high resolution imaging of Io’s surface using adaptive
optics at visible wavelengths.
1. Dr. P. Saranraj M.Sc., M.Phil., Ph.D., NET
Assistant Professor
Department of Microbiology
Sacred Heart College (Autonomous)
Tirupattur, Vellore District.
Mobile: 9994146964
E.mail: microsaranraj@gmail.com
IMMUNOGLOBULINS
2. IMMUNOGLOBULINS
Antibody, also known as an Immunoglobulin (Ig), is a
large, Y-shaped protein (Soluble Glycoprotein) produced
mainly by Plasma cells that is used by the immune
system to neutralize microbial pathogens.
Antibodies are present in the Blood serum,Tissue fluids
and Mucosal surfaces of vertebrate animals.
Each antibody has at least two identical sites that bind to
Antigens.These sites are known as Antigen-binding sites
(or) Paratopes.
The number of Antigen-binding sites on an
antibody is called the Valence of that antibody. For
example, most human antibodies have two binding sites;
therefore, they arc Bivalent.
3. The first use of the term "antibody" occurred in a text
by Paul Ehrlich.
Gerald Maurice Edelman who shared the 1972 Nobel
Prize in Physiology or Medicine for work with Rodney
Robert Porter on the immune system. Edelman's Nobel
Prize-winning research concerned discovery of the
structure of Antibody molecules.
The first evidence that antibodies were contained in
particular serum protein fractions came from a classic
experiment by A.Tiselius and E.A. Kabat in 1939.
Immunoglobulins constitute 20 to 25 % of total serum
protein.
4. STRUCTURE OF IMMUNOGLOBULINS
Gerald Maurice Edelman shared the 1972 Nobel Prize
with Rodney Robert Porter for the discovery of the
structure of Antibody molecules.
A bivalent (arranged in pairs) antibody has the simplest
molecular structure, it is called a Monomer.
Heavy and Light Chains
A typical antibody monomer has 4 protein chains: 2
identical Light chains and 2 identical Heavy chains.
Each Light chain polypeptide usually consists of about 220
amino acids and has a mass of approximately 25,000 Da.
Each Heavy chain consists of about 440 amino acids and
has a mass of about 50,000 to 70,000 Da.
5. Disulfide Bonds
The chains (Light and Heavy chains) are joined by Disulfide
links and other bonds to form aY-shaped molecule.
TheY-shaped molecule is flexible and can assume a T shape.
Variable (V) and Constant Regions (C)
Both Light and Heavy chains contain two different regions.
They are (i)Variable region and (ii) Constant region.
The two sections located at the ends of the “Y” arms are
calledVariable (V) regions.
The Variable region is present in both Light chain (VL) (110
Amino acids) and the Heavy chain (VH) (110Amino acids).
The Variable regions folded together and forms the
Antigen binding site (Paratope).
6. The stem of the antibody monomer and the lower parts of
the arms of the “Y” are called the Constant regions (C).
The Constant region is present in both Light chain (CL) (110
Amino acids) and the Heavy chain (CH) (330 - 440 Amino
acids). Five major types of C regions
There arc, which account for the five major classes of
Immunoglobulins.
Hinge region
The four chains are arranged in the form of a
flexible “Y” with a Hinge region.
The Hinge region allows the antibody molecule to be more
flexible, adjusting to the different spatial
arrangements of Epitopes orAntigenic determinants.
7. Fab region
The top of the Y consists of two Antigen-binding
fragments (Fab) that bind with compatibleAntigens.
Fab regions are composed of bothVariable and Constant
region (MW 45,000 D).
Fc region or Crystallizable Fragments
The stem of the “Y” shaped antibody monomer is called the
Fc region (MW 50,000 D).
Fc regions are important in Immunological reactions.
Fc regions are composed of only Constant region.
Fc region interacts with cell surface receptors
called Fc receptors and some proteins of the complement
system. This property allows antibodies to activate
the immune system.