Cytochrome P-450 from lodderomyces elongisporus: Its purification and some properties of the highly purified protein |
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| Authors: | P Riege W-H Schunck H Honeck H-G Müller |
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| Institution: | Central Institute of Molecular Biology of the Academy of Sciences of GDR, Department of Applied Enzymology, 1115 Berlin, Lindenberger Weg 70 Germany |
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| Abstract: | An effective method, based on the chromatography on ω-aminooctyl Sepharose 4B, for the purification of the alkane-induced cytochrome P-450 is described. The purified cytochrome P-450 was homogeneous in SDS/polyacrylamide gel electrophoresis. In the oxidized state it showed a low spin type absorption spectrum. The reduced CO-complex is characterized by a Soret peak at 447 nm. The alkane hydroxylating enzyme system could be reconstituted combining purified cytochrome P-450 with partially purified NADPH-cytochrome P-450 reductase from the yeast microsomal fraction. |
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| Keywords: | cytochrome cyt |
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