Studies on the red oxidase (cytochrome ) of |
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Authors: | T.Y. Yang P. Jurtshuk |
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Affiliation: | Department of Biology, University of Houston Houston, Texas 77004 USA |
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Abstract: | ![]() In an attempt to isolate and to study the electron transport system of , we have isolated and purified a membrane-bound cytochrome . The cytochrome , purified as a detergent (Triton X-100) and hemoprotein complex, contained 1.6 nmoles heme per mg of protein. Cold-temperature spectrum showed that no other cytochrome was associated with the purified preparation, and electrophoresis revealed that only one type of hemoprotein was obtained. The purified cytochrome reacted with both carbon monoxide and cyanide readily. Only in the reduced form did it combine with carbon monoxide, whereas the oxidized form reacted with cyanide. An “oxygenated” form of the cytochrome was demonstrated to be spectrally distinguishable from both the oxidized and the reduced forms. |
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Keywords: | TMPD SDS sodium dodecylsulfate DEAE diethylaminoethyl |
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