Primary structure of human J chain: alignment of peptides from chemical and enzymatic hydrolyses.

Abstract:

:The primary structure of the J chain from a human Waldenströms 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.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Mole JE,Bhown AS,Bennett JC

doi

10.1021/bi00635a002

subject

Has Abstract

pub_date

1977-08-09 00:00:00

pages

3507-13

issue

16

eissn

0006-2960

issn

1520-4995

journal_volume

16

pub_type

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