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- W1602654647 abstract "During systematic investigations, the adenine-free derivatives of NAD and 3-acetylpyridine-adenine dinucleotide, 3-acetylpyridine mononucleotide and nicotinamide-cytosine dinucleotide were prepared in a pure state and were characterized. A comparison of the absorption spectra of the dihydroderivatives and of the cyanide and sulphite addition compounds indicated that an interaction took place between both heterocyclic bases. The properties of the NAD models were studied under the same conditions with crystalline yeast and liver alcohol dehydrogenase, rabbit-skeletal-muscle and pig-heart lactic dehydrogenase, mitochondrial horse-heart malic dehydrogenase, ox-liver glutamic dehydrogenase and rabbit-skeletal-muscle glyceraldehyde-3-phosphate dehydrogenase. The adenine-free compounds were reduced in all systems but at greatly different rates. The Michaelis constants of some of the coenzyme models and substrates were determined. The values showed that pyrophosphate and adenine parts were important in the binding as well as in the activation. Im Rahmen systematischer Untersuchungen wurden die adeninfreien Verbindungen von Nicotinamid-adenin-dinucleotid und 3-Acetylpyridin-adenin-dinucleotid, das 3-Acetylpyridin-mononucleotid und Nicotinamid-cytosin-dinucleotid rein dargestellt und charakterisiert. Aus dem Vergleich der Absorptionsspektren der Dihydroverbindungen und der Cyanid- und Sulfit-Additionsverbindungen läßt sich eine Wechselwirkung zwischen den beiden heterocyclischen Basen ableiten. Die Wirksamkeit der Nicotinamid-adenin-dinucleotid-Modelle wurde unter gleichartigen Reaktionsbedingungen an kristallisierter Hefe- und Leber-Alkohol-dehydrogenase, Kaninchenskeletmuskel- und Schweineherz-l-Lactat-dehydrogenase, mitochondrialer Pferdeherz-l-Malat-dehydrogenase, Rinderleber-l-Glutamat-dehydrogenase und Kaninchenskeletmuskel-Glycerin-aldehyd-3-phosphatdehydrogenase studiert. Die adeninfreien Verbindungen wurden von allen Systemen, allerdings mit sehr unterschiedlicher Geschwindigkeit, reduziert. Es wurden einige Michaeliskonstanten von Coenzymmodellen und Substraten bestimmt. Die Werte lassen erkennen, daß Pyrophosphat- und Adeninteile sowohl für die Bindung als auch für die Aktivierung eine Rolle spielen können." @default.
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- W1602654647 date "1963-05-01" @default.
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- W1602654647 title "Zum wirkungsmechanismus von dehydrogenasen" @default.
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- W1602654647 doi "https://doi.org/10.1016/0926-6569(63)90106-8" @default.
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