Linked Life Data

1319154

Source:http://linkedlifedata.com/resource/pubmed/id/1319154

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1992-7-17
pubmed:abstractText
An enzyme fraction that catalyzes CTP formation from CDP was purified from pig brain homogenate to a single band on SDS-PAGE. The preparation had a molecular weight of about 36,000 and showed a high activity of phosphorylating CMP and UMP by ATP and turned out to be one of pyrimidine nucleoside monophosphate kinases. It also catalyzes UTP formation from UDP, although rather weakly. These characteristics show that the enzyme species from pig brain homogenate has a rather broad specificity toward phosphate donor in phosphorylating nucleoside monophosphate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
853-61
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Pyrimidine nucleoside monophosphate kinase isolated from pig brain homogenate catalyzes disproportionation of phosphate between two CDP molecules.
pubmed:affiliation
School of Materials Science, Toyohashi University of Technology, Japan.
pubmed:publicationType
Journal Article, In Vitro