Toyo Boseki Kabushiki Kaisha

Noriyuki Hongo

Yoshihisa Kawamura

Kazumi Yamamoto

Shinichi Teshima

Shizuo Hattori

A novel glutamate dehydrogenase derived from the genus Pseudomonas which is specific to L-glutamic acid, requires NAD.sup.+ and NADH as coenzymes, does not act on NADP.sup.+ and NADPH, is with an optimum pH 10.5-11.5 (oxidative deamination), a pH stability of 5-10 (at 25.degree. C.; 20 hours), an optimum temperature of about 60.degree. C. (oxidative deamination) and a molecular weight of about 280,000 (gel filtration) or about 41,000 (SDS-PAGE) and is not activated by ADP. A reagent composition for measuring an amount of ammonia characterized in containing a glutamate dehydrogenase which is not activated by ADP and is NADH-dependent, .alpha.-ketoglutaric acid or a salt thereof and NADH; and a reagent composition wherein urease or creatinine deiminase is further added to the above-mentioned reagent composition.

Reagent composition of glutamate dehydrogenase from pseudomonas

A novel glutamate dehydrogenase is derived from the genus Pseudomonas and is specific to L-glutamic acid, requires NAD.sup.+ and NADH as coenzymes, does not act on NADP.sup.+ and NADPH, has an optimum pH 10.5-11.5 (oxidative deamination), a pH stability of 5-10 (at 25.degree. C.; 20 hours), an optimum temperature of about 60.degree. C. (oxidative deamination) and a molecular weight of about 280,000 (gel filtration) or about 41,000 (SDS-PAGE) and is not activated by ADP.

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Tsuruga, Japan

Noriyuki Hongo