A new assay for glutamate-oxaloacetate transaminase

Hajime Itoh, P. Srere

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

A new method for continuously measuring glutamate-oxaloacetate transaminase (GOT) activity is described. Oxaloacetate produced by GOT from aspartate is condensed with acetyl CoA to form citrate and CoA in a system coupled with citrate synthase. The CoASH formed is measured by its reaction with DTNB. The chromophore formed has a high molar extinction coefficient and absorbs at 412 nm. This method is more sensitive than the usual methods for GOT and produces a visible change in color.

Original languageEnglish
Pages (from-to)405-410
Number of pages6
JournalAnalytical Biochemistry
Volume35
Issue number2
DOIs
Publication statusPublished - 1970

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Oxaloacetic Acid
Transaminases
Glutamic Acid
Assays
Coenzyme A
Dithionitrobenzoic Acid
Citrate (si)-Synthase
Acetyl Coenzyme A
Chromophores
Aspartate Aminotransferases
Citric Acid
Color

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

A new assay for glutamate-oxaloacetate transaminase. / Itoh, Hajime; Srere, P.

In: Analytical Biochemistry, Vol. 35, No. 2, 1970, p. 405-410.

Research output: Contribution to journalArticle

Itoh, Hajime ; Srere, P. / A new assay for glutamate-oxaloacetate transaminase. In: Analytical Biochemistry. 1970 ; Vol. 35, No. 2. pp. 405-410.
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