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Purification and Partial Characterization of Microsomal NADH-Cytochrome b5 Reductase from Higher Plant Catharanthus roseus

Madyastha, KM and Chary, NK and Holla, R and Karegowdar, TB (1993) Purification and Partial Characterization of Microsomal NADH-Cytochrome b5 Reductase from Higher Plant Catharanthus roseus. In: Biochemical and Biophysical Research Communications, 197 (2). pp. 518-522.

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Official URL: http://dx.doi.org/10.1006/bbrc.1993.2509

Abstract

A simple three step procedure was used to purify microsomal NADH-cytochrome b5 (ferricyanide) reductase to homogeneity from the higher plant C. roseus. The microsomal bound reductase was solubilized using zwitterionic detergent-CHAPS. The solubilized reductase was subjected to affinity chromatography on octylamino Sepharose 4B, blue 2-Sepharose CL-6B and NAD+-Agarose. The homogeneous enzyme has an apparent molecular weight of 33,000 as estimated by SDS-PAGE. The purified enzyme catalyzes the reduction of purified cytochrome b5 from C. roseus in the presence of NADH. The reductase also readily transfers electrons from NADH to ferricyanide (Km 56 μM), 2,6-dichlorophenolindophenol (Km 65 μM) and cytochrome Image via cytochrome b5 but not to menadione.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Science.
Department/Centre: Division of Chemical Sciences > Organic Chemistry
Date Deposited: 24 Feb 2011 05:36
Last Modified: 21 Oct 2011 05:47
URI: http://eprints.iisc.ernet.in/id/eprint/35717

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