Purification of bovine liver microsomal NADH-cytochrome reductase using affinity chromatography |
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Authors: | Dorothy A. Schafer Donald E. Hultquist |
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Affiliation: | Department of Biological Chemistry The University of Michigan Ann Arbor, Michigan 48109 USA |
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Abstract: | Microsomal NADH-cytochrome reductase has been purified from bovine liver by an improved procedure which employs affinity chromatography on ADP-agarose in combination with anion exchange chromatography. The reductase was extracted from a 105,000 × microsomal pellet with Triton X-100. The overall purification from isolated microsomes was 98-fold and the yield was 10%. The preparation was nearly homogeneous on SDS-PAGE. This procedure requires less time and effort than previously described procedures. Partially purified cytochrome is also obtained. |
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Keywords: | To whom reprint requests should be addressed. |
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