Studies on human platelet protease activity. Academic Article uri icon

Overview

abstract

  • SOLUBILIZED PROTEIN DERIVED FROM HUMAN PLATELETS WAS FRACTIONATED BY DEAE CELLULOSE COLUMN CHROMATOGRAPHY AND ANALYZED FOR PROTEASE ACTIVITY USING THREE SUBSTRATES: denatured bovine hemoglobin, alpha casein, and purified plasminogen-free human fibrinogen. A protein fraction was found with proteolytic activity which was heat labile and not attributable to plasmin. The activity was not potentiated by cysteine or inhibited by iodoacetamide. Studies of pH optima indicated a broad range of enzyme activity with peaks in both the acid and alkaline region. Cathepsin A activity was detected in the platelet protease fraction by hydrolysis of the synthetic substrate N-carbobenzoxy-alpha-L-glutamyl-L-tyrosine. Similar proteolytic activity was found when the proteins derived from isolated platelet granules were examined. The results indicate that human platelets possess potent intracellular proteolytic enzymes. The relationship of this proteolytic activity to the hemostatic process is discussed.

publication date

  • November 1, 1969

Research

keywords

  • Blood Platelets
  • Peptide Hydrolases

Identity

PubMed Central ID

  • PMC297418

Scopus Document Identifier

  • 0014605652

Digital Object Identifier (DOI)

  • 10.1172/JCI105935

PubMed ID

  • 4237782

Additional Document Info

volume

  • 47

issue

  • 11