Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-1-16
pubmed:abstractText
The hydrolysis and transfer reactions of purified human renal gamma-glutamyltransferase were studied in vitro with glutathione as substrate at pH and substrate concentration reflecting the physiological conditions. The pH optimum ranged from 7.48 to 8.44 for hydrolysis and 7.90 to 8.92 for transfer with glutamine as acceptor. The Michaelis constants for glutathione were 13 microM in hydrolysis and 58 microM in transfer reactions respectively. Inhibition of transfer occurred for glutathione concentrations above 0.4 mM. Various ions, urea, creatinine, uric acid and L-amino acids were shown to have no appreciable effect on both reactions except L-glutamine which acts as an activator on the hydrolysis activity. Taken together, our results, if they are transposable in vivo would be relevant of an enzyme acting like an hydrolase rather than like a transferase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0003-9799
pubmed:author
pubmed:issnType
Print
pubmed:volume
88
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
117-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Human renal gamma-glutamyltransferase hydrolysis and transfer reactions with glutathione as substrate.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't