On the degradation of heparin by human blood platelets.
Human blood platelets are able to degrade heparin from different tissues and species. The main degradation product is an oligosaccharide. Low molecular weight components such as inorganic sulfate or monosaccharides, i.e. products released by exoenzymes are not detected. The in vitro degradation of heparin by the crude enzyme is observed at pHs below 6.5 with an optimum temperature around 37 degrees C. The presence of sulfate in the substrate structure is shown to be essential for the enzyme activity. Since the oligosaccharides formed have only 10 per cent of the anticoagulant activity of the heparins tested, it is conceivable that the platelet enzyme may play an important role in the inactivation of some of the biological properties of heparin.
D001792:Blood Platelets / Q000502:physiology*; D004591:Electrophoresis, Polyacrylamide Gel; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D013045:Species Specificity
D006493:Heparin