Literature DB >> 6869807

A spectrophotometric method for the determination of aminopeptidase activity with leucine dehydrogenase.

S Takamiya, T Ohshima, K Tanizawa, K Soda.   

Abstract

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.

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Year:  1983        PMID: 6869807     DOI: 10.1016/0003-2697(83)90678-4

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  1 in total

1.  Gene cloning, purification, and characterization of thermostable and halophilic leucine dehydrogenase from a halophilic thermophile, Bacillus licheniformis TSN9.

Authors:  S Nagata; S Bakthavatsalam; A G Galkin; H Asada; S Sakai; N Esaki; K Soda; T Ohshima; S Nagasaki; H Misono
Journal:  Appl Microbiol Biotechnol       Date:  1995-12       Impact factor: 4.813

  1 in total

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