Primary structure of a human IgA1 immunoglobulin. I. Isolation, composition, and amino acid sequence of the chymotryptic peptides.
As the initial phase of the determination of the complete covalent structure of a human immunoglobulin A, 52 chymotryptic peptides, ranging in length from 2 to 37 residues, were isolated and characterized from the reduced and carboxymethylated alpha1 heavy chain of the myeloma IgA protein Bur. The peptides were subjected to sequence analysis by the dansylation technique, manual and automatic Edman degradation, and carboxypeptidase digestion. The results, in conjunction with the data on the tryptic and thermolysin peptides and the cyanogen bromide fragments reported in the accompanying papers, established the complete primary structure of a human IgA chain.
D000595:Amino Acid Sequence; D002918:Chymotrypsin; D003488:Cyanogen Bromide; D006801:Humans; D007070:Immunoglobulin A; D007128:Immunoglobulin Fragments / Q000032:analysis; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D007145:Immunoglobulin kappa-Chains; D007461:Iodoacetates; D010446:Peptide Fragments / Q000032:analysis
D007070:Immunoglobulin A; D007128:Immunoglobulin Fragments; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D007145:Immunoglobulin kappa-Chains; D007461:Iodoacetates; D010446:Peptide Fragments; D002918:Chymotrypsin; D003488:Cyanogen Bromide