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Analysis of human C4A and C4B binding to an immune complex in serum.

Abstract：

:Previous studies using isolated complement proteins have shown that more C4A than C4B binds to certain types of immune complexes. However, the in vivo binding of the C4 isoforms to an immune complex has not been investigated in detail and may differ from events when measured with the isolated proteins. We report here the binding of C4A and C4B to an immune complex of bovine serum albumin (BSA) anti-BSA as it occurs in serum. We found that when using the isolated C4 proteins more C4A than C4B bound to the complex, but in serum similar amounts of C4A and C4B were found to bind. Furthermore, these results were not explainable by a difference in activity between isoforms. In an attempt to explain these results a number of unexpected observations were noted. First C4A, but not C4B, bound specifically to a yet unidentified 38-kD serum protein. Second, when both covalent and non-covalent binding was assessed, we found that as serum concentration increased there followed a concomitant decrease in covalent binding and C4B was more affected than C4A. The potential biological significance of these findings is discussed.

journal_name

Clin Exp Immunol

journal_title

Clinical and experimental immunology

authors

Reilly BD

doi

10.1046/j.1365-2249.1999.00940.x

subject

Has Abstract

pub_date

1999-07-01 00:00:00

pages

12-8

issue

1

eissn

0009-9104

issn

1365-2249

pii

cei940

journal_volume

117

pub_type

杂志文章

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