Linked Life Data

3170501

Source:http://linkedlifedata.com/resource/pubmed/id/3170501

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1988-11-8
pubmed:abstractText
The reaction of pig heart mitochondrial and cytosolic aspartate aminotransferases (abbreviated to mAspAT and cAspAT, respectively) with an enzyme-suicide substrate (mechanism-based inhibitor), gostatin (5-amino-2-carboxyl-4-oxo-1,4,5,6-tetrahydropyridine-3-acetic acid) was studied kinetically, by following the spectral change with a micro-stopped-flow apparatus, as well as the inactivation of the enzyme activity. No significant difference in kinetic behavior was observed between mAspAT and cAspAT. From the analysis of time-dependent spectral change, no positive evidence for the existence of spectrophotometrically distinguishable intermediates was obtained. Both the spectral change and the inactivation followed, at least in appearance, simple bimolecular association kinetics, under the conditions studied. However, the second-order rate constant of the spectral change was found to be 1.5 to 2 times as large as that of the inactivation. The effects of pH and temperature on k(on) (the second-order rate constant of the spectral change) were also studied.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
103
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
585-8
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Kinetic studies on the binding of gostatin, a suicide substrate for aspartate aminotransferase, with the isoenzymes from porcine heart mitochondria and cytosol.
pubmed:affiliation
Faculty of Agriculture, Kyoto University.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't