Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1978-6-12
pubmed:abstractText
The strength of the bond between 125I-labelled C1q and immune complexes, Fc piece, dextran sulphate, polyglutamic acid and polylysine has been investigated. The binding of C1q to Fc piece, small molecular weight (less than 10,000) dextran sulphate, polyglutamic acid and polylysine have value; for the functional affinity constant (Ko) in the range of 0.2-1.5 X 10(4) M-1. In contrast the binding of C1q to immune complexes and large molecular weight polyions (greater than 100,000 is much greater and lies in the range 3 X 10(7)--4 X 10(8) M-1. The differences in the binding constants between the two groups can be explained if the Fc piece and small molecular weight compounds bind to only 1 head of the C1q molecule but the immune complexes and large molecules bind to 2 heads. There are probably 6 binding sites on the C1q molecule for dextran sulphate. The enhancement of the binding affinity of C1q by reduction in ionic strength and the reaction with polyions, indicate that ionic groups are present near or within the binding sites.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0019-2805
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
459-63
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1978
pubmed:articleTitle
The reaction between the complement subcomponent C1q, IgG complexes and polyionic molecules.
pubmed:publicationType
Journal Article