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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 19, Number 2
BKCSDE 19(2)
February 20, 1998 

 
Title
Purification and Comparison of NADH-Cytochrome b5 Reductase from Mitochondrial Outer Membrane of Bovine Heart and Turnip
Author
Jae Yang Lee, Young Ho Kim, Sang Jik Lee*
Keywords
Abstract
The NADH-cytochrome b5 reductase (NCBR), a mitochondrial external electron carrier, was purified from bovine heart and turnip and their properties were examined. The mitochondrial outer membranes separated were subjected to NCBR isolation through DEAE-Cellulose ion exchange, DEAE-Sephadex gel chromatography, and hydroxyapatite adsorption chromatography. These processes yielded the purification folds of 88 and 42 and the recovery percentages of 0.2%, 5.67% for turnip and bovine heart, respectively. The molecular weight of the NCBR from the two sources was estimated to be 35,000 using SDS polyacrylamide gel electrophoresis. The Michaelis constant Km and maximum velocity Vmax were determined by measuring the NADH-ferricyanide redox system as well as the NADPH-ferricyanide redox system. The kinetics showed that both NCBRs had higher affinities for NADH than artificial electron-acceptor substrate ferricyanide. Although NADPH had a lower affinity for the enzymes than NADH, this study showed the 2'-phosphate dinucleotide could be used as a substrate.
Page
160 - 164
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