Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-12-21
pubmed:abstractText
Human pregnancy-associated plasma protein A (PAPP-A) inhibited significantly the proteolytic activity of bovine trypsin and human plasmin. Trypsin or plasmin treatment of PAPP-A resulted in the generation of a major 85 kDa component and the rapid cleavage of internal thiol esters. The results indicated that both of these serine proteinases bound in a 1:1 stoichiometry to PAPP-A. The PAPP-A-bound enzymes were found to be enzymatically active towards small synthetic substrates and inaccessible to inactivation by soybean trypsin inhibitor and alpha 1-proteinase inhibitor. The mechanism of proteinase inhibition was likely to be entrapment, as described for alpha 2-macroglobulin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
239
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-55
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Interaction of human pregnancy-associated plasma protein-A with serine proteinases.
pubmed:affiliation
Central Research Laboratory, Postgraduate Physician Training Institute, Novokuznetsk, Russian Federation.
pubmed:publicationType
Journal Article