Literature DB >> 415360

Covalent immunoglobulin assembly in vitro: reactivity of light chain covalent dimers (L2) and blocked light chain monomers.

A R Kazin, S Beychok.   

Abstract

Covalent light chain dimers (L2) and cysteine-blocked L chain monomers readily react with partially reduced heavy (H) chains. A rapid disappearance of these blocked L chain species is followed by the appearance of covalent intermediates-HL, H2, and H2L-leading to fully assembled H2L2. The mechanism of initial disulfide bond formation between heavy and light chains is disulfide interchange.

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Year:  1978        PMID: 415360     DOI: 10.1126/science.415360

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  2 in total

1.  Self-association of human immunoglobulin kappa I light chains: role of the third hypervariable region.

Authors:  F J Stevens; F A Westholm; A Solomon; M Schiffer
Journal:  Proc Natl Acad Sci U S A       Date:  1980-02       Impact factor: 11.205

2.  Alternative pathways of disulfide bond formation yield secretion-competent, stable and functional immunoglobulins.

Authors:  Yechiel Elkabetz; Ayala Ofir; Yair Argon; Shoshana Bar-Nun
Journal:  Mol Immunol       Date:  2008-08-09       Impact factor: 4.407

  2 in total

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