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L-Leucine dehydrogenase purified from Bacillus megaterium and Bacillus sphearicus was used for the determination of serum aminopeptidase activity with L-leucinamide as a substrate. L-Leucine produced by aminopeptidase was determined by measurement of the increase in absorbance at 340 nm caused by the formation of NADH. This method is useful for the kinetic studies of the aminopeptidase and the enzyme assay of a large number of samples. The serum aminopeptidase can be characterized to give some valuable information in clinical diagnosis by comparison of the results obtained by the present method with those by the conventional method with L-leucyl-p-nitroanilide as a substrate.
S Takamiya, and
T Ohshima, and
K Tanizawa, and
K Soda
June 1968,
Clinical chemistry,
S Takamiya, and
T Ohshima, and
K Tanizawa, and
K Soda
January 1962,
Epatologia (Roma),
S Takamiya, and
T Ohshima, and
K Tanizawa, and
K Soda
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S Takamiya, and
T Ohshima, and
K Tanizawa, and
K Soda
April 1954,
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S Takamiya, and
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K Tanizawa, and
K Soda
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S Takamiya, and
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K Soda
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S Takamiya, and
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K Tanizawa, and
K Soda
November 1967,
Clinica chimica acta; international journal of clinical chemistry,
S Takamiya, and
T Ohshima, and
K Tanizawa, and
K Soda
October 1946,
The Journal of biological chemistry,
S Takamiya, and
T Ohshima, and
K Tanizawa, and
K Soda
March 1979,
Clinica chimica acta; international journal of clinical chemistry,
S Takamiya, and
T Ohshima, and
K Tanizawa, and
K Soda
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Plant physiology,
