Activation studies by phospholipids on the purified cytochromec
4:o oxidase ofAzotobacter vinelandii |
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Authors: | Tit-Yee Wong Peter Jurtshuk Jr |
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Institution: | (1) Department of Biology, University of Houston, 77004 Houston, Texas;(2) Present address: Department of Biology, The Johns Hopkins University, 21218 Baltimore, Maryland |
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Abstract: | A modified procedure is described that was used to solubilize and purify the TMPD-dependent cytochromec
4:o oxidase fromAzotobacter vinelandii. Two functional components (Fractions I and V) were obtained after DEAE-cellulose chromatography. Fraction V contained both cytochromec
4 (3.6 nmol/mg protein) and cytochromeo (1.6 nmol/mg protein). This cytochrome oxidase complex oxidized TMPD at moderate rates. Fraction I, a clear greenish-yellow fraction, contained primarily phosphatidylethanolamine with some phosphatidylglycerol. Fraction I itself could not oxidize TMPD, but when it was preincubated with Fraction V, a 2–4-fold stimulation in TMPD oxidase activity occurred. Other authentic micellar phospholipids also readily activited TMPD oxidase activity in Fraction V. Themaximum activation effect obtained with Fraction I was in essence duplicated with purified phosphatidylethanolamine.Dedicated to the memory of David E. Green, a fine gentleman, an excellent scientist, and a true scholar. He will be missed by many of his former colleagues. |
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Keywords: | Cytochrome oxidase Azotobacter vinelandii phospholipid activation cytochromec
4:o oxidase phosphatidylethanolamine TMPD oxidase |
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