The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
DIARYL PYROPHOSPHATASE AND FAD PYROPHOSPHATASE
SHIGERU YAMAWAKI
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JOURNAL FREE ACCESS

1956 Volume 43 Issue 5 Pages 683-689

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Abstract

Diphenyl pyrophosphate is hydrolysed by diaryl pyrophosphatase into two moles of monophenyl phosphate. This enzyme is inactive to flavin adenine dinucleotide, which is in turn split by nucleotide pyro-phosphatase to produce flavin monophosphate and adenylic acid. For either diaryl pyrophosphatase or nucleotide pyrophosphatase there are two isodynamic, acid and alkaline, enzymes. The acid FAD pyro-phosphatase is found in potato extract and the alkaline enzyme in muscle autolysate. Acid diaryl pyrophosphatase contained in potato extract can be obtained free from isodynamic alkaline enzyme, whereas the two isodynamic diaryl pyrophosphatases of the liver, though they could be made free from other phosphatases, are incapable at present, of being separated from each other.
This work was supported in part by a grant from the Ministry of Education, given to Prof. S. Akamatsu, the director of this department.

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© The Japanese Biochemical Society
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