Characterization of trisulfide modification in antibodies

被引：80

作者：

Gu, Sheng ^{[1
]}

Wen, Dingyi ^{[1
]}

Weinreb, Paul H. ^{[1
]}

Sun, Yaping ^{[1
]}

Zhang, Lihe ^{[1
]}

Foley, Susan F. ^{[1
]}

Kshirsagar, Rashmi ^{[1
]}

Evans, David ^{[1
]}

Mi, Sha ^{[1
]}

Meier, Werner ^{[1
]}

Pepinsky, R. Blake ^{[1
]}

机构：

[1] Biogen Idec Inc, Cambridge, MA 02142 USA

来源：

ANALYTICAL BIOCHEMISTRY | 2010年 / 400卷 / 01期

关键词：

Trisulfides; Trisulfides in proteins; Peptide mapping; Posttranslational modification; Disulfide structure; Recombinant antibodies; Natural antibodies; HUMAN GROWTH-HORMONE; MASS-SPECTROMETRY; STRUCTURAL-CHARACTERIZATION; VARIANT; EXPRESSION; STABILITY; SULFIDE; ENGAGE; BONDS; H2S;

D O I：

10.1016/j.ab.2010.01.019

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Trisulfides are a posttranslational modification formed by the insertion of a sulfur atom into a disulfide bond. Although reports for trisulfides in proteins are limited, we find that they are a common modification in natural and recombinant antibodies of all immunoglobulin G (IgG) subtypes. Trisulfides were detected only in interchain linkages and were predominantly in the light-heavy linkages. Factors that lead to trisulfide formation and elimination and their impact on activity and stability were investigated. The peptide mapping methods developed for characterization and quantification of trisulfides should be applicable to any antibody and can be easily adapted for other types of proteins. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：89 / 98

页数：10

共 30 条

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