Linked Life Data

6840049

Source:http://linkedlifedata.com/resource/pubmed/id/6840049

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1983-6-10
pubmed:abstractText
Two closely related but different aminopeptidases from bovine lung have been isolated and characterized. The first aminopeptidase, which removes the N-terminal arginine residue from L-arginyl-L-prolyl-L-proline, bradykinin, and des-[Arg9]-bradykinin, has kininase activity; it has a pH optimum of 8.0, is stimulated by Mn2+, and its molecular weight in dilute buffers is slightly greater than 240,000 daltons. The second aminopeptidase, which converts kallidin to bradykinin, has kinin-converting activity; it has a pH optimum of 6.8, is stimulated by Co2+, and its molecular weight in dilute buffers is 250,000 daltons. The kinin-converting enzyme is blocked from action when the N-terminal penultimate residue is proline.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0013-9432
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21-31
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
A kininase and a kinin-converting enzyme: two distinct alpha aminoacyl peptide hydrolases from bovine lung.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't