Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1982-10-29
pubmed:abstractText
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.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0042-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
86-93
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Acid-stable proteinase inhibitor from the urine of pregnant women, the properties of the highly purified preparation and the isolation of a monospecific antiserum].
pubmed:publicationType
Journal Article, Comparative Study, English Abstract