ピリドキサールリン酸誘導体のGlutamic-Oxaloacetic Transaminaseにたいする補酵素作用
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概要
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The purified glutamic-oxoalacetic apotransaminase extracted from soluble fraction of pig heart was incubated with the phosphopyridoxal oxime. Then the enzyme was precipitated by adding ammonium sulfate to the solution. At higher concentration of the enzyme, it was found that from its ultraviolet absorption spectrum and its pyridoxal phosphate content the oxime combined with apoenzyme remained nearly intact even after the enzymic reaction. At lower concentration, where the reaction rate increased liniearly with an amount of the enzyme, the sodium borohydride was used as the means to see the state of the phosphopyridoxal oxime in the enzyme, and it was found that the oxime in the enyme was cleaved after the transformation with the substrates.
- 日本ビタミン学会の論文
- 1964-02-25