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Purification of bovine liver microsomal NADH-cytochrome reductase using affinity chromatography
Schafer, Dorothy A.; Hultquist, Donald E.
1980-07-16
Citation:Schafer, Dorothy A., Hultquist, Donald E. (1980/07/16)."Purification of bovine liver microsomal NADH-cytochrome reductase using affinity chromatography." Biochemical and Biophysical Research Communications 95(1): 381-387. <http://hdl.handle.net/2027.42/23200>
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 x 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.