An assay for transaminase C is presented in which the pyruvate formed via transamination between cY-ketoisovalerate and alanine is determined using p-dimethylaminobenzaldehyde. This reagent reacts with pyruvate in alkaline solution to form a yellow chromophore having an absorption peak at 420 nm, bu
New method for assay of tyrosine transaminase
β Scribed by Bernard Schepartz
- Publisher
- Elsevier Science
- Year
- 1969
- Tongue
- English
- Weight
- 338 KB
- Volume
- 30
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
2-oxoglutarate aminotransferase, EC 2.6.1.5) activity has been assayed by a number of methods in recent years, including the photometric procedures of Briggs (1) (modified by Canellakis and Cohen (2))) Lin et al. (3), and Diamondstone (4)) the isotopic methods of Weinstein et al. ( 5)) Gabay and George (6), Wurtman and Larin ( 7)) and Litwack and Squires ( 8)) as well as new isotopic and photometric methods recently reported in preliminary form by Fellman et al. ( 9). The multiplicity of methods reflects not so much the dissatisfaction of later investigators with already available methods as it does varying requirements for sensitivity, specificity, speed, handling of multiple samples, interference by other substances present, etc. In our own case, an investigation of the effects of certain phenolic inhibitors on tyrosine transaminase (to be published elsewhere) led to the establishment of yet another photometric method. Our starting point was the discovery of a specific color reaction between arylpyruvates and phenazine methosulfate (10).
π SIMILAR VOLUMES
Glutamate-oxaloacetate transaminase (GOT) (n-aspartate: 2-oxoglutarate aminotransferase, EC 2.6.1.1) is an extensively studied enzyme (1, 2) and its content in sera from a variety of patients has important clinical diagnostic value (3). A large number of methods are available for its determination
In the course of investigat'ing some kinetic properties of relatively crude preparations of tyrosine transaminase (L-tyrosine:2-oxoglutarate aminotransferase, EC 2.6.1.5), it became necessary to use rather low concentrations of enzyme. The concentrations involved were so low that the modified Briggs
Tyrosine hydroxylase can be measured by release of tritiated water from labeled tyrosine, and the assay method has now been modified to allow recovery of 3H2O from the reaction mixture in a much more rapid and less tedious manner than previously possible. In the new method, the tyrosine hydroxylase