Platelet collagen adhesion characterization of collagen glucosyltransferase of plasma membranes of human blood platelets

摘要: Abstract A glucosyltransferase which transfers glucose specifically from UDPG to incomplete heterosaccharide chains of collagen has been purified 20-fold in platelet plasma membranes isolated by the gycerol-lysis technique. The enzyme is inactive with other acceptors and collagen-dependent activity about 5 time greater than endogeneous presence collagen. a pH optimum (5.7) metal requirement (15mM Mn 2+ ) similar that enzymes same sources (HeLa cells, fibroblasts, kidney cortex) activated one-fifth Ca , Mg CO . inhibited aspirin, glucosamine, sylcosamine, sulfhydryl-blocking reagents product-inhibited UDP; range inhibition shown platelet:cologen adhesion may play major role.