The properties of proteins from blood platelets soluble in 0.2 M tris-HCl, pH 8.2 have been studied and more than one thrombin-sensitive protein detected by gel electrophoresis. The most prominent effect of thrombin is on a protein migrating in the beta-globulin region which shows a diminution in amount and a change in the electrophoretic mobility. This protein has been partially purified. The protein fails to produce a precipitin line against anti-whole serum on immunoelectrophoresis or against anti-fibrinogen in starch gel immunoelectrophoresis. It does not contain fibrin-stabilizing factor, factor V or platelet factor III.

This content is only available as a PDF.
© 1969 by American Society of Hematology, Inc.
1969
Sign in via your Institution