Purification and fine structure of reduced coenzyme Q-cytochrome C reductase in the mitochondrial membrane
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<p>For the purpose of revealing the molecular organization of the mitochondrial membrane the authors attempted to clarify the fine structure of reduced coenzyme Q-cytochrome c reductase and also studied how the CoQH2-cyt. c reductase is arranged in the mitochondrial membrane by systematic analyses of fractions from the purification process of CoQH2-cyt. c reductase. 1. Purified CoQH2-cyt. c reductase contained high concentration of cyt. b (9.5 mμmoles per mg protein) and cyt. Cl (4.5 mμmoles per mg protein), and was almost free from cyt. c, a, flavoproteins, primary dehydrogenases and ATPase. The enzyme complex also showed a high specific activity (48 μmoles of cyt. c reduced per mg protein per min at 30°). 2. CoQH2-cyt. c reductase was composed of particles of about 120 Å in diameter with irregular form, some time exhibiting electron opaque cores. In the loose aggregates of the particles, the size of each particle was about 95 Å in diameter. 3. An intimate correlation was observed between the particles of CoQH2cyt. c reductase and those on the surface of the NADH-cyt. c reductase fraction. 4. Regular arrays of uniform particles (about 82 Å in diameter with a center to center distance of about 100 Å) were observed on the surface of the submitochondrial membrane (brown membrane) obtained from beef heart mitochondria by treatment with deoxycholate (0.1 mg / mg protein) and KCl (72 g/l). The correlation between these particles and CoQH2-cyt. c reductase was discussed.</p>
収録刊行物
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- Acta Medicinae Okayama
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Acta Medicinae Okayama 21 (2), 79-89, 1967-04
Okayama University Medical School
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詳細情報 詳細情報について
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- CRID
- 1390572174501827072
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- NII論文ID
- 120002312095
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- NII書誌ID
- AA00041342
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- IRDB
- CiNii Articles