Alteration of Mitochondria with a Protein Modifying Agent
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Beef heart mitochondria were treated with 2, 4-dimethylmaleic anhydride (DMMA). A structural protein fraction was selectively released from the mitochondria by DMMA treatment. When the DMMA to protein ratio was about one to one, ap- proximately 55 % of total protein was released and an increased amount of DMMA showed no further release of protein. Electron micrographs indicated that residue fraction of DMMA treated mitochondria retained a trilaminar arrangement and the inner membrane particles were disappeared from the treated mitochondrial prepara- tions. Approximately 40 % of NADH-cytochrome C reductase and cytochrome oxidase activities were retained in the DMMA treated residues. All of these activities were found in the residues and essentially no activities were recovered in the supernatant. In case of μ-hydroxybutyrate dehydrogenase, DMMA treatment (DMMA: protein= 0.25: 1, mg/mg) gave approximately 50 % decrease in the activity at pH 8.2, and it could be completely recovered if the residues were brought to pH 6.5. Additional treatment with DMMA resulted in loss of the activity and it was only partially recovered by lowered pH. Depletion of lipid from mitochondria by extraction with aqueous acetone caused no substantial effect on the amount of protein released by DMMA treatment. These results may lead to the following conclusions. The structural protein may not be an essential component for the basic architecture of mitochon- drigmembrane but loosely associated with it. It is conceivable that phospholipid is intimately associated with the basic membrane and not with the structural protein in the mitochondrion. Among respiratory enzymes, NADH-cytochrome C reductase and cytochrome oxidase activities are restored in the absence of structural protein.(Supported USPHS Grant GM-12831, AM-14632.)
- Japan Society of Clinical Chemistryの論文
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