[Properties and prospects of practical use of extracellular L-glutamate oxidase from Streptomyces sp. Z-11-6].
The properties of extracellular L-glutamate oxidase, isolated and purified from Streptomyces sp. Z-11-6 (specific activity, 50.8 U/mg protein; yield, 40%), were studied. A photometrical method of determination of activities of alanine- and aspartate aminotransferases, based on the use of the L-glutamate oxidase and peroxidase, has been developed. This method is sufficiently sensitive to be used for the determination of aminotransferase activities in biological fluids. The presence of other amino acids did not interfere with the analysis and had no effect on the results of determination.
Sukhacheva
M V
MV
Biological Faculty, Moscow State University, Vorob'evy gory, Moscow, 119899 Russia. msukhacheva@mail.ru
Zhuravleva
N I
NI
D000410:Alanine Transaminase / Q000032:analysis / Q000378:metabolism; D000594:Amino Acid Oxidoreductases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D001219:Aspartate Aminotransferases / Q000032:analysis / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D013379:Substrate Specificity
D000594:Amino Acid Oxidoreductases; C023061:L-glutamate oxidase; D001219:Aspartate Aminotransferases; D000410:Alanine Transaminase