BIOMAT Database Logo BIOMAT Database Logo

[Nature of the interaction of light-chain immunoglobulins with immobilized heavy chains]. 1984

I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ

UI MeSH Term Description Entries
D007143 Immunoglobulin Heavy Chains The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa. Immunoglobulins, Heavy-Chain,Heavy-Chain Immunoglobulins,Ig Heavy Chains,Immunoglobulin Heavy Chain,Immunoglobulin Heavy Chain Subgroup VH-I,Immunoglobulin Heavy Chain Subgroup VH-III,Heavy Chain Immunoglobulins,Heavy Chain, Immunoglobulin,Heavy Chains, Ig,Heavy Chains, Immunoglobulin,Immunoglobulin Heavy Chain Subgroup VH I,Immunoglobulin Heavy Chain Subgroup VH III,Immunoglobulins, Heavy Chain
D007147 Immunoglobulin Light Chains Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule. Ig Light Chains,Immunoglobulins, Light-Chain,Immunoglobulin Light Chain,Immunoglobulin Light-Chain,Light-Chain Immunoglobulins,Chains, Ig Light,Chains, Immunoglobulin Light,Immunoglobulins, Light Chain,Light Chain Immunoglobulins,Light Chain, Immunoglobulin,Light Chains, Ig,Light Chains, Immunoglobulin,Light-Chain, Immunoglobulin
D007163 Immunosorbent Techniques Techniques for removal by adsorption and subsequent elution of a specific antibody or antigen using an immunosorbent containing the homologous antigen or antibody. Immunoadsorbent Techniques,Immunoadsorbent Technics,Immunosorbent Technics,Immunoadsorbent Technic,Immunoadsorbent Technique,Immunosorbent Technic,Immunosorbent Technique,Technic, Immunoadsorbent,Technic, Immunosorbent,Technics, Immunoadsorbent,Technics, Immunosorbent,Technique, Immunoadsorbent,Technique, Immunosorbent,Techniques, Immunoadsorbent,Techniques, Immunosorbent
D009194 Myeloma Proteins Abnormal immunoglobulins characteristic of MULTIPLE MYELOMA. M Components,Proteins, Myeloma
D004306 Dose-Response Relationship, Immunologic A specific immune response elicited by a specific dose of an immunologically active substance or cell in an organism, tissue, or cell. Immunologic Dose-Response Relationship,Relationship, Immunologic Dose-Response,Dose Response Relationship, Immunologic,Dose-Response Relationships, Immunologic,Immunologic Dose Response Relationship,Immunologic Dose-Response Relationships,Relationship, Immunologic Dose Response,Relationships, Immunologic Dose-Response
D004347 Drug Interactions The action of a drug that may affect the activity, metabolism, or toxicity of another drug. Drug Interaction,Interaction, Drug,Interactions, Drug
D006863 Hydrogen-Ion Concentration The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000042 Absorption The physical or physiological processes by which substances, tissue, cells, etc. take up or take in other substances or energy.
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001667 Binding, Competitive The interaction of two or more substrates or ligands with the same binding site. The displacement of one by the other is used in quantitative and selective affinity measurements. Competitive Binding

Related Publications

I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
Kinetics of interaction of heavy and light chains in immunoglobulins. Use of a sulfhydryl-specific light chain fluorescent probe.
April 1978, The Journal of biological chemistry,
I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
The origin of light and heavy chains of immunoglobulins.
March 1971, Biochemical and biophysical research communications,
I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
Recombination of heavy and light chains from human immunoglobulins.
June 1966, Immunology,
I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
Structure and evolution of light and heavy chains of immunoglobulins.
June 1968, Brookhaven symposia in biology,
I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains.
September 1994, Protein engineering,
I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
Heavy chains of murine splenocyte membrane immunoglobulins: a comparison with the heavy chains of human and toad serum immunoglobulins.
August 1976, Journal of immunogenetics,
I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
Noncovalent association of heavy and light chains in Rana catesbeiana immunoglobulins.
July 1984, Journal of immunology (Baltimore, Md. : 1950),
I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
The interaction of light chain fragments with heavy chain from immunoglobulin G.
February 1972, Biochemical and biophysical research communications,
I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
Myosin heavy chain-light chain recombinations and interactions between the two classes of light chains.
July 1983, The Journal of biological chemistry,
I M Gel'fand, and A R Ibragimov, and O V Rokhlin, and A I Slesarev, and A G Tonevitskiĭ
Biosynthesis of immunoglobulins: the separate classes of polyribosomes synthesizing heavy and light chains.
January 1967, Journal of molecular biology,
Copied contents to your clipboard!