Determination of the primary structure of a mouse IgG2a immunoglobulin. Amino-acid sequence of the H4 cyanogen-bromide fragment.
The complete amino acid sequence of CNBr fragment H4 of the murine immunoglobulin MOPC 173 (IgG2a,chi) 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 CH1 domain, the hinge region and the beginning of CH2. Sequence comparisons suggest that the CH1 domain is highly conserved in evolution, and allows the definition of two additional isotypic-specific regions.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002460:Cell Line; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D003619:Dansyl Compounds; D006801:Humans; D007074:Immunoglobulin G / Q000032:analysis*; D007145:Immunoglobulin kappa-Chains / Q000032:analysis; D051379:Mice; D009194:Myeloma Proteins / Q000032:analysis*; D010446:Peptide Fragments / Q000032:analysis; D013045:Species Specificity; D014357:Trypsin
D000596:Amino Acids; D003619:Dansyl Compounds; D007074:Immunoglobulin G; D007145:Immunoglobulin kappa-Chains; D009194:Myeloma Proteins; D010446:Peptide Fragments; D002918:Chymotrypsin; D014357:Trypsin; D003488:Cyanogen Bromide