A new assay for l-aspartate: 2-oxoglutarate aminotransferase
โ 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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โฆ 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.
๐ SIMILAR VOLUMES
## Electrophoretic and kinetic characterization of two phenotypes of soluble cytoplasmic ~-aspartate:2-oxoglutarate aminotransferase in human liver tissues Two phenotypes of soluble cytoplasmic ~-aspartate:2-oxoglutarate aminotransferase (AST, EC 2.6.1. l), sAST 1 and sAST 2-I , were partially puri
cause no continuous assay for the detection of free phos-A new continuous coupled uv-spectrophotometric phate had been developed that is sensitive yet also conassay is described for two phosphate-releasing envenient and cost effective. Of the continuous assays zymes, aspartate transcarbamylase and A
We designed a rapid, homogeneous assay for human aspartate aminotransferase (AST) isoenzymes, by a selective proteolysis of soluble AST (s-AST), using chymotrypsin and protease 401. The linearity of mitochondrial (m-AST) was elongated up to 4000 U/I. m-AST values from the human liver, and determined