Linked Life Data

495321

Source:http://linkedlifedata.com/resource/pubmed/id/495321

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1979-12-27
pubmed:abstractText
Two kinin forming enzymes were extracted from bovine spleen and separated from cathepsin B1 and B2 by DEAE-Cellulose chromatography. Since these catheptic kininogenases were found to release kinins from kininogens at acidic pH's, these were named acid kininogenase I and II. The presence of SH compounds was not necessary for I to have a kinin forming activity, while it was necessary for II. These have only minor difference for electrophoretic behaviors as can be seen, e.g., from a small difference in pI values, but could be separated by polyacrylamide gel electrophoresis. Their production of kinins from bovine crude bradykininogen was highly reproducible. Kininogenase I was proved to react on bovine HMW kininogen and also to release some kinin from LMW kininogen and leukokininogen. From the study of several substrates, these enzymes were revealed to have very low tryptic and little esterolytic activities and to have affinity to some hydrophobic amino acids.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-2598
pubmed:author
pubmed:issnType
Print
pubmed:volume
120A
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
335-49
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
Substrate specificities of acid kininogenases.
pubmed:publicationType
Journal Article