[Monoamine oxidase. 12. Substrate specificity of monoamine oxidase in the rabbit brain and liver].
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In this paper, we report the inhibition constants obtained with N-cyclopropyl-5,6-dimethoxytryptamine and with N-cyclopropyl-6,7-dimethoxytryptamine on the activity of beef plasma amineoxidase. The inhibition constants are respectively: 0.3 x 10(-3) M and 0.65 x 10(-3) M. A dixon graph of the enzymic oxidation of benzylamine indicates a non-competitive inhibition of the enzyme by these dimethoxytryptamines.
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The molybdenum cofactor has been isolated in an oxidized inactive form from purified molybdoenzymes. The isolated material is shown to be a novel pterin. The active cofactor is presumably composed of molybdenum and a reduced form of the pterin.
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