VOPROSY MEDITSINSKOI KHIMII (ISSN 0042-8809)

Acid-stable proteinase inhibitor from the urine of pregnant women, the properties of the highly purified preparation and the isolation of a monospecific antiserum

   
Ogloblina O.G., Galstian N.A., Karpitskii V.V., Kuzina R.A., Paskhina T.S.
PubMed Id: 7113061
Year: 1982  Volume: 28  Issue: 4  Pages: 86-93
Two highly purified forms of acid-stable proteinase inhibitor from urine of pregnant women with nephropathies (Mr 22000 and 32000, ASI-22 and ASI-32, respectively) were obtained. The preparations were homogenous in molecular mass and polymorphous in molecular charge (pI from 3.9 to 4.2). ASI-22 an ASI-32 effectively inhibited trypsin and chymotrypsin (Ki approximately 1 x 10(-8)-1 x 10(-9) M, ka approximately 10(5)M-1 sec-1, kd approximately 3 x 10(-4) sec-1) by the permanent mechanism of action. Both forms inhibited the esterase activity of pancreatic pig elastase by the progressive mechanism of action (ki approximately 1 x 10(4)M-1 min-1 at 37 degrees). Rabbit monospecific antiserum to total ASI-22 and ASI-32 preparation was obtained 1 ml of the anti-ASI-serum contained 95 micrograms of antibodies. Total ASI preparations was immunochemically homogenous and had antigenic similarity to inter-alpha-trypsin inhibitor from human plasma.
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Ogloblina O.G., Galstian N.A., Karpitskii V.V., Kuzina R.A., Paskhina T.S. (1982) Voprosy meditsinskoi khimii, 28(4), 86-93.
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