Immunoinhibition of ristocetin-induced platelet aggregation. Academic Article uri icon

Overview

abstract

  • Human platelets washed and fixed in paraformaldehyde aggregate in the presence of the antibiotic ristocetin and normal plasma. This aggregation response is abolished after digestion of the fixed platelets with chymotrypsin. Antisera to fixed washed platelets were produced in rabbits and absorbed with chymotrypsin-treated, fixed washed platelets. Monovalent Fab fragments obtained from the isolated gamma-globulin fractions of the antisera blocked ristocetin-induced aggregation of fixed washed platelets in buffer and normal platelets in platelet-rich plasma. By double-antibody immunoprecipitation, it was shown that the antibody which blocked the ristocetin reaction interacted with a platelet membrane surface protein of mol wt 155,000. The results suggest that the glycoprotein I complex on the surface of the human platelet mediates ristocetin-induced von Willebrand factor-dependent platelet aggregation.

publication date

  • January 1, 1977

Research

keywords

  • Chymotrypsin
  • Platelet Aggregation
  • Ristocetin

Identity

PubMed Central ID

  • PMC333341

Scopus Document Identifier

  • 0017334325

Digital Object Identifier (DOI)

  • 10.1172/JCI108612

PubMed ID

  • 299747

Additional Document Info

volume

  • 59

issue

  • 1