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Purification of the nitrogenase proteins from Clostridium pasteurianum
Authors:Man-Yin W Tso  Torbj  rn Ljones and R H Burris
Institution:

Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin, Madison, Wisc. 53706, U.S.A.

Abstract:A method is described for the purification of the nitrogenase proteins from Clostridium pasteurianum by two polyethylene glycol precipitations and chromatography on columns of DEAE-cellulose, Sephadex G-100 and Sephadex G-200. The Mo-Fe protein and the Fe protein have been purified 70–80-fold from the crude extract, and they appear essentially pure when tested by anaerobic polyacrylamide gel electrophoresis.
Keywords:MES  2-(N-morpholino)ethanesulfonic acid
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