Abstract：
:The assignment of disulfide bonds in human J chain and its covalent pairing with immunoglobulin M was determined under conditions which minimize disulfide bond interchange. We show that in J chain the three intradisulfide bridges are formed between Cys 12 and 100, Cys 71 and 91, and Cys 108 and 133. Previous reports [reviewed by Koshland, M. E. (1985) Annu. Rev. Immunol. 3, 425-453] have proposed that cysteines 12, 14, or 68 were linked to the penultimate cysteine 575 of two mu chain tails. In this work, we demonstrate that cysteines 14 and 68 are disulfide-bridged to mu chains. A revised, albeit putative, model of J chain folding is presented which takes into account the correct disulfide pairing and the predictive secondary structure assignment.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Frutiger S,Hughes GJ,Paquet N,Lüthy R,Jaton JCdoi
10.1021/bi00165a014subject
Has Abstractpub_date
1992-12-22 00:00:00pages
12643-7issue
50eissn
0006-2960issn
1520-4995journal_volume
31pub_type
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