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Optical assay of pyruvate carboxylase in crude liver homogenates

โœ Scribed by J. Berndt; B. Messner; T. Turkki; E. Weissmann

Publisher
Elsevier Science
Year
1978
Tongue
English
Weight
262 KB
Volume
86
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

A technique to measure the activity of pyruvate carboxylase spectrophotometritally in crude liver homogenates is described. The assay is based on the transformation of oxaloacetate, which is formed during the carboxylation reaction, into citrate in the presence ofexcess acetyl CoA and citrate synthase. After removal of pyruvate with KBH, and of protein with HCIO,, citrate is cleaved with citrate lyase into oxaloacetate and acetate, and oxaloacetate then is measured spectrophotometrically.

Optimal concentrations of pyruvate, Mg*+, ATP, and KHCO, for the carboxylation reaction and the V,, were in good correlation with the data found by others using ["Clpyruvate.

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A new spectrophotometric assay method of xanthine oxidase applicable to the crude tissue homogenate containing uricase was presented in this paper. By adding potassium 2,4-dihydroxy-6-carboxy-1,3,5-triazine (potassium oxonate) (0.1 mM) to the crude xanthine oxidase reaction system, uric acid was sto