[Effect of the proteinase isolated from a fungus on the kallikrein-kinin system].
Carboxyl proteinase (CP) with the isoelectric point of 6.3-6.4 was isolated from a fungus at the Laboratory of Enzymology of the All-Union Research Technological Institute of Antibiotics and Enzymes and its effect on the kallikrein-kinin system and trypsin caseinolytic activity was studied. Four lots of the preparation with the activity of 1116 to 2300 milk coagulating units per 1 mg were used. The kininogenase activity of kallikrein, bradykinin and trypsin was determined with the routine biological procedures and the trypsin caseinolytic activity was determined with the Kunitz method and the diffusion method on casein-containing agar. It was shown that CP inhibited the kininogenase activity of kallikrein in the secretion of the salivary glands of man and crystalline trypsin in aqueous media and blood serum. It also inactivated the bradykinin constrictor effect on the smooth muscle tissue of the uterus horn in rats. CP had a capacity for inhibiting the caseinolytic activity of crystalline trypsin. Possible use of CP in treatment of patients with diseases accompanied by impairment of the kallikrein-kinin system (increased activity) is discussed.
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D000818:Animals; D001920:Bradykinin / Q000037:antagonists & inhibitors / Q000097:blood; D002268:Carboxypeptidases / Q000302:isolation & purification / Q000494:pharmacology*; D004347:Drug Interactions; D005260:Female; D005658:Fungi / Q000201:enzymology*; D006801:Humans; D007610:Kallikreins / Q000037:antagonists & inhibitors / Q000097:blood*; D007705:Kinins / Q000097:blood*; D009130:Muscle, Smooth / Q000187:drug effects; D051381:Rats; D014357:Trypsin / Q000097:blood; D014361:Trypsin Inhibitors
D007705:Kinins; D014361:Trypsin Inhibitors; D002268:Carboxypeptidases; D007610:Kallikreins; D014357:Trypsin; D001920:Bradykinin
Vliianie proteinazy, vydelennoĭ iz griba, na kallikrein-kininovuiu sistemu.