BIOMAT Database Logo BIOMAT Database Logo

Experimental evidence of the flexibility of immunoglobulin G molecules. 1972

L A Tumerman, and Y A Zagyanskii, and R S Nezlin

UI MeSH Term Description Entries
D007074 Immunoglobulin G The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B. Gamma Globulin, 7S,IgG,IgG Antibody,Allerglobuline,IgG(T),IgG1,IgG2,IgG2A,IgG2B,IgG3,IgG4,Immunoglobulin GT,Polyglobin,7S Gamma Globulin,Antibody, IgG,GT, Immunoglobulin
D007140 Immunoglobulin Fab Fragments Univalent antigen-binding fragments composed of one entire IMMUNOGLOBULIN LIGHT CHAIN and the amino terminal end of one of the IMMUNOGLOBULIN HEAVY CHAINS from the hinge region, linked to each other by disulfide bonds. Fab contains the IMMUNOGLOBULIN VARIABLE REGIONS, which are part of the antigen-binding site, and the first IMMUNOGLOBULIN CONSTANT REGIONS. This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN. Fab Fragment,Fab Fragments,Ig Fab Fragments,Immunoglobulins, Fab Fragment,Fab Immunoglobulin Fragments,Immunoglobulin Fab Fragment,Immunoglobulins, Fab,Fab Fragment Immunoglobulins,Fab Fragment, Immunoglobulin,Fab Fragments, Immunoglobulin,Fragment Immunoglobulins, Fab,Fragment, Fab,Immunoglobulin Fragments, Fab
D008239 Lysine An essential amino acid. It is often added to animal feed. Enisyl,L-Lysine,Lysine Acetate,Lysine Hydrochloride,Acetate, Lysine,L Lysine
D008433 Mathematics The deductive study of shape, quantity, and dependence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed) Mathematic
D008961 Models, Structural A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed) Model, Structural,Structural Model,Structural Models
D010206 Papain A proteolytic enzyme obtained from Carica papaya. It is also the name used for a purified mixture of papain and CHYMOPAPAIN that is used as a topical enzymatic debriding agent. EC 3.4.22.2. Tromasin
D010434 Pepsin A Formed from pig pepsinogen by cleavage of one peptide bond. The enzyme is a single polypeptide chain and is inhibited by methyl 2-diaazoacetamidohexanoate. It cleaves peptides preferentially at the carbonyl linkages of phenylalanine or leucine and acts as the principal digestive enzyme of gastric juice. Pepsin,Pepsin 1,Pepsin 3
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D002850 Chromatography, Gel Chromatography on non-ionic gels without regard to the mechanism of solute discrimination. Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography
D003619 Dansyl Compounds Compounds that contain a 1-dimethylaminonaphthalene-5-sulfonyl group. Dimethylaminonaphthalenesulfonyl Compounds,Compounds, Dansyl,Compounds, Dimethylaminonaphthalenesulfonyl

Related Publications

L A Tumerman, and Y A Zagyanskii, and R S Nezlin
Structure and flexibility of individual immunoglobulin G molecules in solution.
March 2004, Structure (London, England : 1993),
L A Tumerman, and Y A Zagyanskii, and R S Nezlin
Flexibility of immunoglobulin G molecules as established by fluorescent polarisation measurements.
November 1969, Immunochemistry,
L A Tumerman, and Y A Zagyanskii, and R S Nezlin
Segmental flexibility of immunoglobulin G antibody molecules in solution: a new interpretation.
November 1981, Biochemistry,
L A Tumerman, and Y A Zagyanskii, and R S Nezlin
Segmental flexibility of immunoglobulin M molecules.
January 1972, Immunochemistry,
L A Tumerman, and Y A Zagyanskii, and R S Nezlin
Interactions between immunoglobulin G molecules.
August 2010, Immunology letters,
L A Tumerman, and Y A Zagyanskii, and R S Nezlin
The shape of immunoglobulin G molecules in solution.
April 1972, Proceedings of the National Academy of Sciences of the United States of America,
L A Tumerman, and Y A Zagyanskii, and R S Nezlin
Electron microscopic evidence for the axial rotation and inter-domain flexibility of the Fab regions of immunoglobulin G.
September 1983, Journal of molecular biology,
L A Tumerman, and Y A Zagyanskii, and R S Nezlin
Concerning the axial rotational flexibility of the Fab regions of immunoglobulin G.
March 1989, Journal of molecular biology,
L A Tumerman, and Y A Zagyanskii, and R S Nezlin
Existence of the large molecules of immunoglobulin G with another component.
February 1988, Nihon juigaku zasshi. The Japanese journal of veterinary science,
L A Tumerman, and Y A Zagyanskii, and R S Nezlin
Conversion of incomplete antibodies to direct agglutinins by mild reduction: evidence for segmental flexibility within the Fc fragment of immunoglobulin G.
June 1977, Proceedings of the National Academy of Sciences of the United States of America,
Copied contents to your clipboard!