Linked Life Data

6105894

Source:http://linkedlifedata.com/resource/pubmed/id/6105894

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1980-11-20
pubmed:abstractText
gamma-Glutamyltransferase (GGT) from the liver and transplantable hepatoma of rats was purified 130- and 170-fold, respectively. The properties of the enzymatic preparations obtained were studied. The optimum pH for the transferase reaction between L-gamma-glutamyl-p-nitroanilide (5 mM) and glycyl-glycine (50 mM) was 8.0--8.2, while that for the auto-transferase reaction (without glycyl-glycine) amounted to 9.3--9.5. The isoelectric points of GGT from the liver correlated with the pH 3.9, 4.2 and 4.4 whereas those of hepatoma enzyme with the pH 5.7, 6.0 and 7.0 GGT obtained from both sources were equally specific for various acceptors at the pH 8.1 and 7.0. It has been shown that metotrexate (0.9 mM) and folic acid (3.5 mM) inhibited both enzymes by 50%.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0365-9615
pubmed:author
pubmed:issnType
Print
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
58-60
pubmed:dateRevised
2008-10-8
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
[Partial purification and certain properties of gamma-glutamyltransferase from rat liver and hepatoma].
pubmed:publicationType
Journal Article, English Abstract