In:
Pathophysiology of Haemostasis and Thrombosis, S. Karger AG, Vol. 21, No. 6 ( 1991), p. 353-359
Abstract:
We describe here a new antiplatelet glycoprotein (GP) lb monoclonal antibody (MoAb) designated OP-Fl (IgGlκ). Both OP-Fl and a well-characterized anti-GPIb MoAb, AP-1, totally abolished ristocetin-induced von Willebrand factor (vWF) binding to platelets and desialylated vWF binding to platelets at an IgG concentration of 2–8 μg/ml. AP-1 also blocked snake venom botrocetin-induced vWF binding at a similar IgG concentration, whereas OP-Fl had a minimal effect on botrocetin-induced binding. At a higher IgG concentration (150 μg/ml), OP-Fl inhibited botrocetin-induced binding by 50%. AP-1 (IgG) did not interfere with binding of [ 〈 sup 〉 125 〈 /sup 〉 I]OP-F1 (IgG) to platelets. Thus, the epitope involved in the binding of OP-Fl or AP-1 appears to be quite different. These results suggest that the vWF binding site(s) on the GPIb molecule generated by these inducers is in close proximity but not completely identical.
Type of Medium:
Online Resource
ISSN:
1424-8832
,
1424-8840
Language:
English
Publisher:
S. Karger AG
Publication Date:
1991
detail.hit.zdb_id:
2081182-2
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