DISULFIDE BOND ASSIGNMENT IN HUMAN J-CHAIN AND ITS COVALENT PAIRING WITH IMMUNOGLOBULIN-M

被引：52

作者：

FRUTIGER, S

HUGHES, GJ

PAQUET, N

LUTHY, R

JATON, JC

机构：

[1] UNIV GENEVA, MED CTR, DEPT MED BIOCHEM, 1 RUE MICHEL SERVET, CH-1211 GENEVA 4, SWITZERLAND

[2] SWISS INST EXPTL CANC RES, CH-1066 EPALINGES, SWITZERLAND

来源：

BIOCHEMISTRY | 1992年 / 31卷 / 50期

关键词：

D O I：

10.1021/bi00165a014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 9 1, 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.

引用

页码：12643 / 12647

页数：5

共 41 条

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