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The effect of deoxycholate on enzymes with electron transport function from Rhodospirillum rubrum

โœ Scribed by Boll, M.


Publisher
Springer-Verlag
Year
1969
Weight
608 KB
Volume
68
Category
Article
ISSN
0003-9276

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โœฆ Synopsis


The effect of deoxycholate on a number of enzymatic activities with electron transport function from the particulate fraction of Rhodospirillum rubrum has been studied.

  1. The activities are differently inactivated by DOC 1, the NADH oxidase system being the most sensitive-and ~qADH dehydrogenase the least sensitive enzymatic activity. NADH-and succinate-cytochrome e-reductase are Mso rapidly inactivated.

  2. DOC/protein ratios smaller than those which lead to an inactivation stimulate NADH-and succinate-cy~oehrome c-rednctase. The activities are increased by over 1O0 percent. The stimulated activities are stable and are found to be still membrane bound.

  3. NADH dehydrogenase with menadione as electron acceptor is stimulated by appr. 180 percent. The elevated activity is not stable. No increase in activity is found when DCPIP or ferrieyanide are used as electron acceptors.

  4. ~qADH dehydrogenase is partly (45 percent) solubilized by treatment with DOC. The activities can be separated by either fractionation with ammonium sulfate or by gelfiltration with Sephadex. The solubilized portion has a 4--5 fold higher specific activity than the untreated sample. The separated activities are both unstable, the solubilized portion being inactivated more rapidly.

Zusammen/assung. Der Einflul3 yon

Desoxyeholat auf eine Reihe yon enzymatischen Aktivit~ten mit Elektronentransportfunktion aus der Partikelfraktion yon 1L rubrum wurde untersueht. 1. Die Enzyme werden durch D0C unterschiedlich inaktiviert. Das NADH-Oxydasesystem ist die empfindliehste, NADH-dehydrogenase ist die stabilste Aktivit~t. NADH-und Succinat-Cytochrom c-Reduetase werden ebenfalls stark inaktiviert. 2. Ein niedrigeres Verh~ltnis DOC/Protein als das, welches zu einer Inaktivierung ffihrt, stimuliert die Aktivit~ten yon NADH-und Succinat-Cytochrom e-Reductase. Beide Aktivit~ten werden um mehr als 100~ gesteigert. Die erhShten Aktivit~ten sind stabil und sie sind darfiber hinaus noch vollst~ndig membrangebunden. 3. IqADH-Dehydrogenase mit Menadion als Electronenaeceptor wird um ca. 180~ stimuliert. Diese erhShte Aktivit~t ist nieht stabil. Mit DCPIP oder Ferricyanid als Elektronenaceeptor wird keine Stimulierung der Aktivit~t gefunden.


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