A method for the synthesis of N6-(2-aminoethyl)-NAD+ is given. The binding of this NAD+ derivative to different soluble and insoluble supports and the direct coupling of NAD' to epoxyactivated Sepharose are described. Proofs are given that NAD+ is bound through the amino group in 6-position and the NAD' derivative through the aliphatic amino group of the side chain.Non-enzymic reduction of the bound coenzyme to an almost quantitative extent is possible in all cases, but the enzymic reduction is largely influenced by the support. While N6-(2-aminoethyl)-NAD + coupled to soluble dextran is nearly completely reducible by different dehydrogenases with a velocity of about 40% of that for free NAD+, the coenzyme bound to different insoluble matrices is very slowly reduced. Only 5% of the coenzyme derivative bound to BrCN-activated Sepharose are reducible, but 40% when it is bound through a spacer. From capacity determinations evidence is given that, even in this coenzyme gel, only those coenzyme molecules are useful in affinity chromatography which are on the surface of the gel grains; it is supposed that this may be due to the slow diffusion of an enzyme into the inner parts of an affinity gel.

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1909 beschrieb Dimroth eine alkalikatalysierte Umlagerung von 1-substituierten 5-Aminotriazol-Derivaten zu Isomeren mit dem Substituenten an der Aminogruppe. Eine entsprechende Reaktion beobachtet man bei allen N-substituierten Heterocyclen, die in a-Stellung zum alkylierten N-Atom eine Aminogruppe tragen. Quartare 1-Derivate von Adenin isomerisieren z. B. zu den an

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