BINDING-PROPERTIES OF FIBRINOGEN RECEPTOR GPIIB-IIIA PURIFIED FROM HUMAN ERYTHROLEUKEMIA-CELLS
Citation
K. Yoshimura et al., BINDING-PROPERTIES OF FIBRINOGEN RECEPTOR GPIIB-IIIA PURIFIED FROM HUMAN ERYTHROLEUKEMIA-CELLS, Biochemical and molecular medicine, 56(2), 1995, pp. 166-171
Categorie Soggetti
Medicine, Research & Experimental",Biology
SICI code
1077-3150(1995)56:2<166:BOFRGP>2.0.ZU;2-B
Abstract
Large amounts (2.3 mg) of an inactive form of the glycoprotein GPIIb-I
IIa were obtained in highly purified form from 7-liter cultures of hum
an erythroleukemia (HEL) cells. The purified GPIIb-IIIa was converted
to an activated form after its immobilization to 96-well plastic plate
s. The binding of fibrinogen to the activated GPIIb-IIIa was investiga
ted using 24 kinds of RGD peptides and showed that the IC50 values of
these peptides correlated with those obtained with activated platelets
. These findings indicated that the binding properties of the activate
d GPIIb-IIIa from HEL cells are quite similar to those of the platelet
s. (C) 1995 Academic Press, Inc.