The covalent structure of a human gamma G-immunoglobulin. VII. Amino acid sequence of heavy-chain cyanogen bromide fragments H1-H4. 1970

B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman

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
D007136 Immunoglobulins Multi-subunit proteins which function in IMMUNITY. They are produced by B LYMPHOCYTES from the IMMUNOGLOBULIN GENES. They are comprised of two heavy (IMMUNOGLOBULIN HEAVY CHAINS) and two light chains (IMMUNOGLOBULIN LIGHT CHAINS) with additional ancillary polypeptide chains depending on their isoforms. The variety of isoforms include monomeric or polymeric forms, and transmembrane forms (B-CELL ANTIGEN RECEPTORS) or secreted forms (ANTIBODIES). They are divided by the amino acid sequence of their heavy chains into five classes (IMMUNOGLOBULIN A; IMMUNOGLOBULIN D; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M) and various subclasses. Globulins, Immune,Immune Globulin,Immune Globulins,Immunoglobulin,Globulin, Immune
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
D002852 Chromatography, Ion Exchange Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins. Chromatography, Ion-Exchange,Ion-Exchange Chromatography,Chromatographies, Ion Exchange,Chromatographies, Ion-Exchange,Ion Exchange Chromatographies,Ion Exchange Chromatography,Ion-Exchange Chromatographies
D002918 Chymotrypsin A serine endopeptidase secreted by the pancreas as its zymogen, CHYMOTRYPSINOGEN and carried in the pancreatic juice to the duodenum where it is activated by TRYPSIN. It selectively cleaves aromatic amino acids on the carboxyl side. Alpha-Chymotrypsin Choay,Alphacutanée,Avazyme
D003486 Cyanides Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical. Cyanide,Isocyanide,Isocyanides
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino
D014357 Trypsin A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4. Tripcellim,Trypure,beta-Trypsin,beta Trypsin

Related Publications

B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
May 1968, Biochemistry,
B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
May 1968, Biochemistry,
B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
January 1971, Biochemistry,
B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
May 1968, Biochemistry,
B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
August 1967, The Biochemical journal,
B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
November 1975, European journal of biochemistry,
B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
January 1971, Biochemistry,
B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
June 1986, The Journal of biological chemistry,
B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
April 1977, Biochemistry,
B A Cunningham, and U Rutishauser, and W E Gall, and P D Gottlieb, and M J Waxdal, and G M Edelman
February 1970, European journal of biochemistry,
Copied contents to your clipboard!