The amino acid sequence of a human immunoglobulin G3m(g) pFc' fragment. 1977

T E Michaelsen, and B Frangione, and E C Franklin

Amino acid sequence analysis of the pFc' fragment obtained by pepsin digestion of an IgG3; G3m(g) human myeloma protein HER shows it to consist of 112 residues. It starts at position 334 (gamma1 numbering), contains eight residues of the Cgamma2 region, and the whole Cgamma3 domain. Comparison with the sequence of gamma1 shows five differences including an extra Met at 397. Each is accountable by a single base substitution. The sequence is identical to that of a G3m(b0) molecule except for the previously noted allotype related Tyr/Phe exchange at position 436. The high degree of homology (95%) among gamma-chain subclasses suggests a recent diversification.

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
D007126 Immunoglobulin Allotypes Allelic variants of the immunoglobulin light chains (IMMUNOGLOBULIN LIGHT CHAINS) or heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) encoded by ALLELES of IMMUNOGLOBULIN GENES. Allotypes, Immunoglobulin,Allotypic Antibodies,Antibodies, Allotypic,Ig Allotypes,Allotype, Ig,Allotype, Immunoglobulin,Allotypes, Ig,Allotypic Antibody,Antibody, Allotypic,Ig Allotype,Immunoglobulin Allotype
D007128 Immunoglobulin Fragments Partial immunoglobulin molecules resulting from selective cleavage by proteolytic enzymes or generated through PROTEIN ENGINEERING techniques. Antibody Fragment,Antibody Fragments,Ig Fragment,Ig Fragments,Immunoglobulin Fragment,Fragment, Antibody,Fragment, Ig,Fragment, Immunoglobulin,Fragments, Antibody,Fragments, Ig,Fragments, Immunoglobulin
D007141 Immunoglobulin Fc Fragments Crystallizable fragments composed of the carboxy-terminal halves of both IMMUNOGLOBULIN HEAVY CHAINS linked to each other by disulfide bonds. Fc fragments contain the carboxy-terminal parts of the heavy chain constant regions that are responsible for the effector functions of an immunoglobulin (COMPLEMENT fixation, binding to the cell membrane via FC RECEPTORS, and placental transport). This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN. Fc Fragment,Fc Fragments,Fc Immunoglobulin,Fc Immunoglobulins,Ig Fc Fragments,Immunoglobulin Fc Fragment,Immunoglobulins, Fc,Immunoglobulins, Fc Fragment,Fc Fragment Immunoglobulins,Fc Fragment, Immunoglobulin,Fc Fragments, Ig,Fc Fragments, Immunoglobulin,Fragment Immunoglobulins, Fc,Fragment, Fc,Fragments, Ig Fc,Immunoglobulin, Fc
D007142 Immunoglobulin gamma-Chains Heavy chains of IMMUNOGLOBULIN G having a molecular weight of approximately 51 kDa. They contain about 450 amino acid residues arranged in four domains and an oligosaccharide component covalently bound to the Fc fragment constant region. The gamma heavy chain subclasses (for example, gamma 1, gamma 2a, and gamma 2b) of the IMMUNOGLOBULIN G isotype subclasses (IgG1, IgG2A, and IgG2B) resemble each other more closely than the heavy chains of the other IMMUNOGLOBULIN ISOTYPES. Immunoglobulins, gamma-Chain,Immunoglobulin gamma-Chain,gamma Immunoglobulin Heavy Chain,gamma Immunoglobulin Heavy Chains,gamma-1-Immunoglobulin Heavy Chain,gamma-2a-Immunoglobulin Heavy Chain,gamma-2b-Immunoglobulin Heavy Chain,gamma-Chain Immunoglobulins,Heavy Chain, gamma-1-Immunoglobulin,Heavy Chain, gamma-2a-Immunoglobulin,Heavy Chain, gamma-2b-Immunoglobulin,Immunoglobulin gamma Chain,Immunoglobulin gamma Chains,Immunoglobulins, gamma Chain,gamma 1 Immunoglobulin Heavy Chain,gamma 2a Immunoglobulin Heavy Chain,gamma 2b Immunoglobulin Heavy Chain,gamma Chain Immunoglobulins,gamma-Chain, Immunoglobulin,gamma-Chains, Immunoglobulin
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
D009194 Myeloma Proteins Abnormal immunoglobulins characteristic of MULTIPLE MYELOMA. M Components,Proteins, Myeloma
D003488 Cyanogen Bromide Cyanogen bromide (CNBr). A compound used in molecular biology to digest some proteins and as a coupling reagent for phosphoroamidate or pyrophosphate internucleotide bonds in DNA duplexes. Bromide, Cyanogen
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

Related Publications

T E Michaelsen, and B Frangione, and E C Franklin
March 1976, Immunochemistry,
T E Michaelsen, and B Frangione, and E C Franklin
June 1986, Journal of biochemistry,
T E Michaelsen, and B Frangione, and E C Franklin
December 1968, Proceedings of the National Academy of Sciences of the United States of America,
T E Michaelsen, and B Frangione, and E C Franklin
September 1978, Journal of immunology (Baltimore, Md. : 1950),
T E Michaelsen, and B Frangione, and E C Franklin
August 1968, The Journal of biological chemistry,
T E Michaelsen, and B Frangione, and E C Franklin
August 1968, The Journal of biological chemistry,
T E Michaelsen, and B Frangione, and E C Franklin
June 1974, Biochemistry,
T E Michaelsen, and B Frangione, and E C Franklin
August 1970, Biochemistry,
T E Michaelsen, and B Frangione, and E C Franklin
February 1972, Immunochemistry,
T E Michaelsen, and B Frangione, and E C Franklin
May 1968, Biochemistry,
Copied contents to your clipboard!