[Thermostable leukocyte alpha-glycoprotein: immunochemical study and enzyme activity research].
Using immunochemical analysis with standard antisera, leukocyte thermostable alpha-glycoprotein (LT alpha G) was shown to be distinct from lactoferrin, lysozyme, and fibronectin. The determination of peroxidase and nonspecific elastase in immune precipitates of LT alpha G gave negative results. Affinity sorption of LT alpha G onto the pus protein component was revealed. Purified LT alpha G had amidolytic activity in response to a substrate for elastase (p-nitroanilide succinyl-trialanyl). The ability of LT alpha G to cause the hydrolysis of substrates for thrombin, kallikrein, plasmin was investigated. The identity of LT alpha G and granulocyte elastase is suggested.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D004355:Drug Stability; D006023:Glycoproteins / Q000097:blood*; D006801:Humans; D006868:Hydrolysis; D007120:Immunochemistry; D005779:Immunodiffusion; D007700:Kinetics; D007962:Leukocytes / Q000032:analysis* / Q000201:enzymology; D010196:Pancreatic Elastase / Q000097:blood; D010544:Peroxidases / Q000097:blood; D013379:Substrate Specificity
D006023:Glycoproteins; D010544:Peroxidases; D010196:Pancreatic Elastase
Leĭkotsitarnyĭ termostabil'nyĭ al'fa-glikoproteid: immunokhimicheskoe izuchenie i issledovanie fermentnoĭ aktivnosti.