Linked Life Data

3568629

Source:http://linkedlifedata.com/resource/pubmed/id/3568629

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-6-8
pubmed:abstractText
The binding properties of activated C4 to immune complexes (ovalbumin-rabbit IgG antiovalbumin) were studied by using 125I-IgG in the immune complexes or performing the C4 binding assays in the presence of 14C-iodoacetamide. High molecular weight complexes formed between C4 and IgG could be detected by the incorporation of 14C-iodoacetamide in the -SH group generated in the nascent C4b during the activation process. The same complexes with an apparent molecular weight of 180,000 daltons were detected when the immune aggregates contained 125I-IgG. Two-dimensional SDS-PAGE analysis of the C4b-IgG covalent complexes indicated: In the absence of control proteins, the complexes are formed by the alpha'-chain of C4b and the H chain of the antibody. The alpha'-H complexes are 36% sensitive to hydroxylamine and 64% resistant. This is consistent with the presence of two populations of C4, which are not equivalent in their covalent binding with immune complexes. Covalent complexes C4-C4b or C4b(like)-C4b(like) are generated during the C4 activation and they are detected as alpha-alpha' or alpha-alpha complexes, respectively. Interaction of C4b with the L chain of the antibody molecule also seems to occur, but to a lesser extent than with the H chain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0253-5076
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Formation of covalent complexes between the fourth component of human complement and IgG immune aggregates.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't