Some Properties of Pig Kidney-cortex Aldehyde Reductase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1980 Nov 1

PMID 7016111

Citations 7

Authors

F F Morpeth

F M Dickinson

Affiliations

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Abstract

Aldehyde reductase was purified from pig kidney cortex to homogeneity by a new procedure. The molecular weight of the enzyme was estimated by sedimentation equilibrium to be 43 700 and by gel electrophoresis in the presence of sodium dodecyl sulphate to be 41 700. The enzyme is clearly a monomer. The enzyme preparation contained no significant quantities of zinc, manganese or copper and had no essential histidine or thiol groups. Changes in the absorption and fluorescence spectra of NADPH were observed on formation of the enzyme-NADPH complexes. Large changes in the fluorescence spectra were also observed in the presence of sodium barbitone or Warfarin. These changes were used as the basis of active-site titrations, which showed that the enzyme had one active site per molecule. The dissociation constants of NADPH and NADP+ from binary complexes with the enzyme were estimated in spectrophotometric titrations.

Citing Articles

Kinetic studies of the mechanism of pig kidney aldehyde reductase.

Morpeth F, Dickinson F Biochem J. 1981; 193(2):485-92.

PMID: 7030310 PMC: 1162630. DOI: 10.1042/bj1930485.

The kinetic mechanism of the major form of ox kidney aldehyde reductase with D-glucuronic acid.

Daly A, Mantle T Biochem J. 1982; 205(2):381-8.

PMID: 6814425 PMC: 1158491. DOI: 10.1042/bj2050381.

Purification and characterization of the multiple forms of aldehyde reductase in ox kidney.

Daly A, Mantle T Biochem J. 1982; 205(2):373-80.

PMID: 6753832 PMC: 1158490. DOI: 10.1042/bj2050373.

Molar absorptivity and A 1% 1cm values for proteins at selected wavelengths of the visible and ultraviolet regions. XXIII.

Kirschenbaum D Appl Biochem Biotechnol. 1984; 9(2):187-206.

PMID: 6476824 DOI: 10.1007/BF02798752.

Purification and characterization of an enzymically active cleavage product of pig kidney aldehyde reductase.

Cromlish J, Flynn T Biochem J. 1983; 209(3):597-607.

PMID: 6409073 PMC: 1154136. DOI: 10.1042/bj2090597.

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