Linked Life Data

92447

Source:http://linkedlifedata.com/resource/pubmed/id/92447

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1980-2-15
pubmed:abstractText
The acid-stable trypsin inhibitor of human serum and urine is released in vivo by limited proteolysis from the high molecular weight, acid-labile inter-alpha-trypsin inhibitor. When complexed with trypsin, both this acid-stable, active derivative and the inter-alpha-trypsin inhibitor can be degraded in vitro by prolonged digestion with trypsin to a low molecular weight "minimal" inhibitor. This minimal trypsin inhibitor was sequenced and found to be homologous to the known Kunitz-type inhibitors (e.g. the basic trypsin-kallikrein inhibitor from bovine organs). This indicates that the antitryptic activity of the big inter-alpha-trypsin inhibitor is due to a Kunitz-type domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0018-4888
pubmed:author
pubmed:issnType
Print
pubmed:volume
360
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1285-96
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Kunitz-type proteinase inhibitors derived by limited proteolysis of the inter-alpha-trypsin inhibitor, I. Determination of the amino acid sequence of the antitryptic domain by solid-phase Edman degradation.
pubmed:publicationType
Journal Article, Comparative Study