Primary structure of human J chain: alignment of peptides from chemical and enzymatic hydrolyses.
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Mole JE, Bhown AS, Bennett JC
Primary structure of human J chain: alignment of peptides from chemical and enzymatic hydrolyses.
Biochemistry. 1977 Aug 9;16(16):3507-13.
- PubMed ID
- 407930 [ View in PubMed]
- Abstract
The primary structure of the J chain from a human Waldenstroms IgM protein has been determined using a combination of automated and conventional Edman degradative procedures. Eighty-five percent of the sequence was established with peptides isolated from tryptic digests of carboxyamidomethylated and citraconylated J chain, many of which were sequenced completely. Alignment of the tryptic fragments was achieved with peptides generated by chymotrypsin and limited acid hydrolyses. The j chain consits of 129 amino acids and a single oligosaccharide structure linked to asparagine at positon 43 of the sequence. The molecular weight, including 7.5% carbohydrate by weight, is 16 422. The location and arrangement of three half-cystines could be deduced from previous studies, whereas the pairing of the remaining five disulfide bonds still needs to be clarified.