COENZYME ACTIVITY OF PYRIDOXAL PHOSPHATE DERIVATIVES ON GLUTAMICOXALOACETIC TRANSAMINASE

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概要

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• 1. Isonicotinoylhydrazone, oxime, thiosemicarbazone, hydrazone, phenylhydrazone, semicarbazone and thiazolidine combined with penicillamine of pyridoxal phophate activated glutamic-oxaloacetic apotransaminase.2. From the absorption spectra and pyridoxal phosphate content of the enzyme it was found that oxime itself combined with apo-glutamic-oxaloacetic transaminase.3. At higher concentrations of the enzyme, it was found from its ultraviolet absorption spectrum, its pyridoxal phosphate content and the detection of the coenzyme by paper chromatography that the bound oxime remained nearly intact even after the enzyme reaction. At lower concentrations of the enzyme, where the reaction rate increased linearly with the amount of the enzyme, however, it was found by using NaBH4 as the means to see the state of bound oxime that the oxime was decomposed after the enzyme reaction.

• 日本ビタミン学会の論文

著者

• 牧野 堅

  Department of Biochemistry, The Jikei University School of Medicine Tokyo

• 村上 安子

  Department of Medicinal Chemistry, Tokyo Jikei-kai Medical School

関連論文

• COENZYME ACTIVITY OF PYRIDOXAL PHOSPHATE DERIVATIVES ON GLUTAMICOXALOACETIC TRANSAMINASE
• Study on the Pyridoxal Kinase of Mouse Brain

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