Interaction between rat serum phosphorylcholine binding protein and platelet activating factor.
Biochem Biophys Res Commun
; 167(2): 444-9, 1990 Mar 16.
Article
em En
| MEDLINE
| ID: mdl-2322233
ABSTRACT
The binding of rat serum phosphorylcholine binding protein (PCBP) to platelet activating factor (PAF) has been demonstrated using a HPLC-gel filtration technique. The bulk of the bound [3H]-PAF eluted with a higher molecular weight species of PCBP, possibly an aggregated form of PCBP. A smaller amount of [3H]-PAF co-eluted with the major monomeric species of PCBP. Formation of the PCBP-PAF complex was calcium dependent and could be inhibited by phosphorylcholine, suggesting the involvement of the phosphorylcholine binding site on PCBP. Binding of albumin and alpha 1-acid glycoprotein to PAF was not affected by phosphorylcholine or calcium. The specificity of this binding may explain the inhibitory effect of PCBP and related phosphorylcholine binding proteins on PAF induced aggregation of platelets.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fosforilcolina
/
Fator de Ativação de Plaquetas
/
Proteínas de Transporte
/
Colina
Limite:
Animals
Idioma:
En
Revista:
Biochem Biophys Res Commun
Ano de publicação:
1990
Tipo de documento:
Article
País de afiliação:
Canadá