PMID: 3769931Oct 15, 1986Paper

Purification and properties of tauropine dehydrogenase from the shell adductor muscle of the ormer, Haliotis lamellosa

European Journal of Biochemistry
G Gäde

Abstract

Tauropine dehydrogenase (tauropine:NAD oxidoreductase) was purified from the shell adductor muscle of the ormer, Haliotis lamellosa. The enzyme was found to utilize stoichiometrically NADH as co-enzyme and pyruvate and taurine as substrates producing tauropine [rhodoic acid; N-(D-1-carboxyethyl)-taurine]. The enzyme was purified to a specific activity of 463 units/mg protein using a combination of ammonium sulphate fractionation, ion-exchange and affinity chromatography. The relative molecular mass was 38,000 +/- 1000 when assessed by gel filtration on Ultrogel AcA 54 and 42,000 +/- 150 by electrophoresis on 5-10% polyacrylamide gels in the presence of 1% sodium dodecyl sulphate; the data suggest a monomeric structure. Tauropine and pyruvate were found to be the preferred substrates. Among the amino acids tested for activity with the enzyme, only alanine is used as an alternative substrate, but with a rate less than 6% of the enzyme activity with taurine. Of the oxo acids tested, 2-oxobutyrate and 2-oxovalerate were also found to be substrates. Apparent Km values for the substrates NADH, pyruvate and taurine are 0.022 +/- 0.003 mM, 0.64 +/- 0.07 mM and 64.7 +/- 5.4 mM, respectively, at pH 7.0 and for the products, NAD+ and taur...Continue Reading

Citations

Aug 1, 1996·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·N KannoY Sato
May 26, 2005·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Nobuhiro Kan-NoMinoru Sato
Mar 13, 1999·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·N Kan-noY Sato
Jul 30, 1999·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·N Kan-noE Nagahisa
Feb 15, 1989·European Journal of Biochemistry·E C Webb

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