Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1976-7-6
pubmed:abstractText
Gamma-glutamyl transpeptidase transfers the gamma-glutamyl moiety of glutathione to a variety of acceptor amino acids. Through the operation of the gamma-glutamyl-cyclotransferase cycle, this enzyme has been implicated in the transport of amino acids into cells, especially the cells of the proximal tubules of kidney. It has been reported to be present in rabbit erythrocytes. However, using white cell-free preparations, we have not been able to demonstrate the presence of gamma-glutamyl transpeptidase in human or rabbit erythrocytes either by measuring the utilization of GSH or by following the formation of the product. 14C-L-methionine was used as acceptor amino acid, and the formation of gamma-glutamyl-14C-L-methionine was followed. Using similar conditions, we have been able to demonstrate the presence of gamma-glutamyl transpeptidase in human and rabbit leukocytes and in human kidney. In contrast to a previous report, we were unable to find the accumulation of 5-oxoproline, an intermediate of the gamma-glutamyl-cyclotransferase pathway in human red cells incubated in Krebs-Ringer solution. Immunologic studies demonstrated that human red cell membranes contained no protein antigenically similar to kidney gamma-glutamyl transpeptidase. Thus our studies indicated that in human and rabbit erythrocytes, the gamma-glutamyl transpeptidase-cyclotransferase pathway was not operative.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
645-50
pubmed:dateRevised
2009-10-27
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Studies on gamma-glutamyl transpeptidase in human and rabbit erythrocytes.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.