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A new assay for l-aspartate: 2-oxoglutarate aminotransferase

โœ Scribed by Toshiharu Yagi; Hiroyuki Kagamiyama; Shigeki Ohtawara; Kenji Soda; Mitsuhiro Nozaki


Publisher
Elsevier Science
Year
1979
Tongue
English
Weight
380 KB
Volume
100
Category
Article
ISSN
0003-2697

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โœฆ Synopsis


A new enzymatic assay for aspartate aminotransferase is presented. The 2-oxoglutarate formed in transamination between L-glutamate and oxalacetate was determined in a system coupled with hydroxyglutarate dehydrogenase and NADH by following a decrease in absorbance at 340 nm. The method allowed accurate determination of the initial velocity of the reaction, which was proportional to the enzyme concentration. The Michaelis constants of pig heart cytosolic aspartate aminotransferase for L-glutamate and oxalacetate and the amino acceptor specificity using L-glutamate as an amino donor were determined. The method was applicable to the determination of the enzyme activity in various materials including rat serum -and bacterial crude extract.


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