JBC, Vol. 254, Issue 8, 2859-2864, Apr, 1979
Primary structure of a human IgA1 immunoglobulin. III. Isolation, composition, and amino acid sequence of the thermolysin peptides
Y. S. Liu, T. L. Low and F. W. Putnam
As part of the strategy for determination of the complete covalent
structure of a human IgA immunoglobulin, 66 peptides were isolated from a
thermolysin digest of reduced and carboxymethylated IgA alpha1 chain Bur
and were purified. They range in length from 2 to 24 residues. Some of the
peptides have been characterized and sequenced in order to supply needed
information that was not obtained from the chymotryptic and tryptic
peptides. These thermolysin peptides provide much necessary data to produce
a rigorous proof for the primary structure of the human alpha1 chain. The
remaining peptides from the thermolysin digest whose amino acid composition
and NH2-terminal residues were sufficient to identify them unequivocally
have also been assigned in the structure. They supply additional
information that helps remove ambiguity in the structure, and they provide
useful data about the profile of the peptide bonds that are susceptible to
thermolysin digestion.
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