The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Seya, T.
Right arrow Articles by Atkinson, J. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Seya, T.
Right arrow Articles by Atkinson, J. P.

The Journal of Immunology, Vol 136, Issue 11 4152-4156, Copyright © 1986 by American Association of Immunologists

ARTICLES

Location of the interchain disulfide bonds of the fourth component of human complement (C4): evidence based on the liberation of fragments secondary to thiol-disulfide interchange reactions

T Seya, S Nagasawa and JP Atkinson

Treatment of human C4 with chemical denaturants and heat produces rapid, autolytic peptide bond cleavage of the alpha-chain. These alpha- chain fragments are linked to the parent C4 molecule through disulfide bonds. On more prolonged heating, however, there is liberation of several peptides, including the beta-chain, the gamma-chain, and a C- terminal alpha-chain fragment. This reaction is inhibited by iodoacetamide. By using a fluorescent thiol reagent and 14C- iodoacetamide, the thiol group present on each peptide was analyzed. The results suggest that the thiol residue exposed by cleavage of the thioester bond induces thiol-disulfide interchange reactions to liberate the peptides. Based on the identification of fragments liberated, the kinetics of their appearance, their sulfhydryl content, and the reported primary structure of human C4, a model of the interchain disulfide bonds is proposed in which the amino terminal portion of the alpha-chain is disulfide-linked to both the beta- and gamma-chains, whereas the carboxyl terminal portion of the alpha-chain is disulfide-linked to only the gamma-chain.


This article has been cited by other articles:


Home page
 ScienceHome page
X. Han, M. Jin, K. Breuker, and F. W. McLafferty
Extending top-down mass spectrometry to proteins with masses greater than 200 kilodaltons.
Science, October 6, 2006; 314(5796): 109 - 112.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
K. Shida, I. Shiratori, M. Matsumoto, Y. Fukumori, A. Matsuhisa, S. Kikkawa, S. Tsuji, H. Okamura, K. Toyoshima, and T. Seya
An Alternative Form of IL-18 in Human Blood Plasma: Complex Formation with IgM Defined by Monoclonal Antibodies
J. Immunol., June 1, 2001; 166(11): 6671 - 6679.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 1986 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 1986 by The American Association of Immunologists, Inc. All rights reserved.