Sep 1, 1975

Studies on D-tetrose metabolism. VI. Crystallization and some properties of D-erythrulose reducatase from beef liver

Journal of Biochemistry
K Uehara, T Tanimoto

Abstract

D-Erythrulose reductase of beef liver was crystallized from ammonium sulfate solution at pH 8.17. The crystals are needle-shaped. The enzyme protein contains 851 amino acid residues per mole of the enzyme: Lys28, His11, Arg52, Asp79, Thr58, Ser56, Glu68, Pro20, Gly80, Ala107, Val112, Met24, Ile31, Leu88, Tyr7, Phe22, Trp4, and Cys4. The enzyme is inactivated by exposure to temperatures below 12degrees. The inactivation is accelerated by increasing the salt concentration and decreasing the enzyme concentration. The pH of the medium also has a pronounced effect, the maximum stability of the enzyme is obtained at pH 8.5. NADP+ protected the enzyme from cold inactivation at all stages of the process and also afforded protection against inactivation by heat and pH. The cold inactivation of the enzyme is accompanied by dissociation of the enzyme protein to subunits.

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Mentioned in this Paper

Alcohol Oxidoreductases
Tetroses
NADP
Drug Stability
Bos indicus
Polymorphism, Crystallization
Hydrogen-Ion Concentration
Ketoses
Liver
TRPC4

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