Linked Life Data

6270118

Source:http://linkedlifedata.com/resource/pubmed/id/6270118

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1981-12-15
pubmed:abstractText
A novel isozyme of lactate dehydrogenase is detected in various cells transformed by the Kirsten murine sarcoma virus (KiMSV). This isozyme, designated LDHk, is strongly inhibited by physiological concentrations of oxygen, in an apparently cooperative fashion. LDHk is inhibited by guanosine triphosphate and related compounds, in a noncompetitive fashion. LDHk is found with both 35,000- and 22,000-dalton subunits, although these probably cleave from a 57,000-dalton precursor. In studies utilizing a temperature-sensitive transforming gene mutant of the Kirsten sarcoma virus, we find in vivo expression of LDHk is also temperature-sensitive. In studies using either crude cell-free extracts or purified LDHk, we find the enzyme from cells infected with a temperature-sensitive transforming gene mutant of KiMSV is thermolabile relative to that from wild type KiMSV-infected cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
256
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10583-91
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
LDHk, a uniquely regulated cryptic lactate dehydrogenase associated with transformation by the Kirsten sarcoma virus.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't