Binding of rat serum phosphorylcholine binding protein to platelets.
Biochim Biophys Acta
; 1034(3): 281-4, 1990 Jun 20.
Article
em En
| MEDLINE
| ID: mdl-2364084
ABSTRACT
Rat serum phosphorylcholine binding protein (PCBP), a normal component of rat serum, inhibits in vitro aggregation of rat, rabbit and human platelets by interacting with platelets. In the present study, we have demonstrated the calcium-dependent, specific and saturable binding of 125I-PCBP to rat, rabbit and human platelets. Scatchard analysis of the binding data reveal a class of specific high-affinity binding sites with Kd values of 45.2 +/- 14.9, 26.1 +/- 8.3 and 32.2 +/- 9.9 nM on rat, rabbit and human platelets, respectively. These platelets also expressed a high capacity for binding to 125I-PCBP. The binding of 125I-PCBP to platelets was calcium- and time-dependent, and could be inhibited by phosphorylcholine (IC50 = 5.6 microM). Occupation of these binding sites by PCBP may be responsible for inhibition of platelet aggregation.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Plaquetas
/
Proteína C-Reativa
Limite:
Animals
/
Humans
/
Male
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
1990
Tipo de documento:
Article
País de afiliação:
Canadá