title: [Nature of the proteinase activated by the contact factor in human blood plasma].
abstract: The nature of protamine splitting proteinase, which was formed after treatment of human blood plasma by kaolin or silicone (aerosile), was studied. The activated enzyme did not exhibite the properties of thrombin and plasmin in reactions with specific substrates. Kyninogenic, TAME (N-tosyl-d-,l-arginine methyl ester)-esterase and protamine splitting activities were inherent in the proteinase; these properties enabled to group the enzyme with blood kallikreins. The purified preparations of human blood plasma kallikrein hydrolyzed protamine sulphate even at 10 mcg/ml concentration. alpha2-macroglobulin inhibited the protamine splitting activity of the plasma kallikrein.
mesh_terms: D004789:Enzyme Activation; D005174:Factor XII; D006801:Humans; D007610:Kallikreins / Q000097:blood; D007616:Kaolin; D007704:Kininogens; D010447:Peptide Hydrolases / Q000097:blood*; D011479:Protamines; D012822:Silicon Dioxide; D014106:Tosylarginine Methyl Ester
chemical_list: D007704:Kininogens; D011479:Protamines; D007616:Kaolin; D012822:Silicon Dioxide; D005174:Factor XII; D014106:Tosylarginine Methyl Ester; D010447:Peptide Hydrolases; D007610:Kallikreins
vernacular_title: Izuchenie prirody proteinazy, aktiviruiushcheĭsia kontaktnym faktorom, v plazme krovi cheloveka.