Open AccessDetermination of the Primary Structure of a Mouse IgG2a Immunoglobulin
Author(s) -
ROCCASERRA José,
MILILI Michéle,
FOUGEREAU Michel
Publication year - 1975
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1975.tb02478.x
Subject(s) - residue (chemistry) , protein primary structure , antibody , amino acid residue , immunoglobulin heavy chain , sequence (biology) , peptide sequence , fragment (logic) , amino acid , chemistry , peptide , peptide fragment , heavy chain , immunoglobulin light chain , stereochemistry , biochemistry , microbiology and biotechnology , biology , genetics , mathematics , gene , algorithm
The complete amino acid sequence of CNBr fragment H4 of the murine immunoglobulin MOPC 173 (IgG2a,x) has been determined, thus completing the sequence determination of the entire heavy chain. The H4 fragment contains 150 residues, and extends from residue 105 to residue 254 of the heavy chain, which appears thus to be composed of 447 amino acids residues. This fragment contains the end of the V region, the switch peptide, the C H 1 domain, the hinge region and the beginning of C H 2. Sequence comparisons suggest that the C H 1 domain is highly conserved in evolution, and allows the definition of two additional isotypic‐specific regions.