Kinetic studies of the lipid requirement of mitochondrial cytochromec oxidase |
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Authors: | W L Zahler Sidney Fleischer |
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Institution: | (1) Department of Molecular Biology, Vanderbilt University, 37203 Nashville, Tennessee |
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Abstract: | The lipid requirement of cytochromec oxidase was reinvestigated using both acetone and phospholipase A to deplete mitochondria of lipid. Removal of lipid resulted in a decrease in both the apparentK
m for cytochromec and apparentV
max when compared to control mitochondria. Addition of phospholipid to the assay mixture reactivated the enzyme. For both treatments theK
m returned to the control value. With phospholipase A treated mitochondria theV
max increased to near the control value, while acetone extracted mitochondria could be restored to aV
max of 1/2 that of the control. Detergent does not substitute for phospholipid and inhibits the reactivation with phospholipid.This research was supported in part by United States Public Health Service Research Grant AM-14632 and a Grant-in-Aid of the American Heart Association. |
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Keywords: | |
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