PURIFICATION AND PARTIAL CHARACTERIZATION OF A RAT-KIDNEY ALDEHYDE DEHYDROGENASE THAT OXIDIZES RETINAL TO RETINOIC ACID

被引：55

作者：

LABRECQUE, J ^{[1
]}

BHAT, PV ^{[1
]}

LACROIX, A ^{[1
]}

机构：

[1] UNIV MONTREAL,CLIN RES INST MONTREAL,DEPT MED,NUTR & CANC LAB,MONTREAL H2W 1R7,PQ,CANADA

来源：

BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE | 1993年 / 71卷 / 1-2期

关键词：

ALDEHYDE DEHYDROGENASE; VITAMIN-A; RETINAL; RETINOIC ACID; KIDNEY;

D O I：

10.1139/o93-013

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A NAD-dependent aldehyde dehydrogenase (EC 1.2.1.3) which catalyzes the oxidation of retinal to retinoic acid was purified to homogeneity from rat kidney by using Affi-Gel blue affinity chromatography and chromatofocusing, followed by Mono-Q anion-exchange chromatography. The apparent molecular weight of the native enzyme determined by size-exclusion fast protein liquid chromatography was 140 000. Sodium dodecyl sulfate - polyacrylamide gel electrophoresis gave a subunit molecular weight of 53 000. The isoelectric point as measured by chromatofocusing was 8.5. The enzyme also catalyzed the oxidation of acetaldehyde, but showed much lower K(m) value for the retinal substrate. We suggest that aldehyde dehydrogenase found in the kidney may be a specific retinal dehydrogenase, involved in vitamin A metabolism.

引用

页码：85 / 89

页数：5

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