Feb 1, 1976

Isolation and some properties of NAD+ reductase of the green photosynthetic bacterium Prosthecochloris aestuarii

Journal of Biochemistry
Y ShioiM Nishimura

Abstract

NAD+ reductase of the green photosynthetic bacterium Prosthecochloris aestuarii was isolated and purified by ammonium sulfate fractionation, DEAE-cellulose column chromatography, and Sephadex G-200 gel filtration. This enzyme is an FAD-containing flavoprotein and has absorption maxima at 485 (shoulder0 452, 411, and 385 nm (the 411 nm band is due to cytochrome). The molecular weight of the enzyme as determined by gel filtration using Sephadex G-200 is 119,000. The enzyme catalyzes the reduction of NAD+ and NADP+ by photoreduced spinach ferredoxin or reduced benzyl viologen...

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Mentioned in this Paper

Spinach preparation
Sephadex G 200
Ferredoxin
NADPH-Ferrihemoprotein Reductase
Sodium 2,6-Dichloroindophenol
Rotenone
Neutrophil Actin Dysfunction
Spinacia oleracea
Ferredoxin Activity
Flavoproteins

About this Paper

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