INVESTIGATION OF THE MECHANISM OF FIBRINOLYSIS

Abstract

In in vitro studies bovine pancreatic ribonuclease has been found to inhibit the depolymerization and hydrolysis of bovine fibrin by plasmin of human origin. The human plasmin utilized was observed to enhance the nuclease enzyme activity of bovine pancreatic ribonuclease. Studies made on the role of heparin and ribonuclease in fibrinolysis have indicated that heparin inhibits the antiplasmin activity of ribonuclease. In addition, it has been found that heparin in low con centration (1 - 10 NIH units) induces liquefaction of fibrin clots in vitro without added plasmin. Bovine pancreatic ribonuclease will inhibit this effect of heparin. Dilute acid hydrolysis of bovine pancreatic ribonuclease (0.01N - 0.075N hydrochloric acid) results in the loss of the nuclease activity of ribonuclease but not the antiplasmin activity of ribonuclease. The data obtained are discussed in terms of the mechanism of fibrinolysis and the functions of ribonuclease and heparin.

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Document Details

Document Type
Technical Report
Publication Date
Jun 30, 1963
Accession Number
AD0419066

Entities

People

  • Joseph B. Michaelson

Tags

DTIC Thesaurus Topics

  • Acids
  • Amino Acids
  • Anticoagulants
  • Biological Sciences
  • Blood Coagulation
  • Blood Coagulation Factors
  • Chemistry
  • Enzymes
  • Fibrin
  • Fibrinolysis
  • Government Procurement
  • Hydrochloric Acid
  • Inhibition
  • Molecules
  • Nucleic Acids
  • Ribonuclease
  • Ribonucleic Acids

Fields of Study

  • Computer science

Readers

  • Molecular and Cellular Biochemistry
  • Trauma Surgery or Emergency Medicine.