Oriental Yeast Co., Ltd.

Japan as Represented by Director General of Agency of Industrial Science

Hirokazu Matsukawa

Tuyosi Fujita

Kohji Uchida

Yushi Matuo

Osamu Oka

Kentaro Miyazaki

Kousaku Murata

Tsuyoshi Fujita

Yoshio Ando

Shigeyuki Kawai

Tairo Oshima

Yuhsi Matsuo

Tadayuki Imanaka

Shoichi Tomisako

Chikako Terashima

The present invention provides a novel process for preparing nicotinamide adenine dinucleotide phosphate (NADP). The process of the present invention comprises performing phosphorylation using a polyphosphoric acid or a salt thereof and nicotinamide adenine dinucleotide (NAD) as substrates in the presence of a polyphosphate-dependent NADkinase from a, wherein the reaction solution contains 0.1-15% by weight of the polyphosphoric acid or a salt thereof, and 5-150 mM of a divalent metal ion.

Process for preparing nicotinamide adenine dinucleotide phosphate(NADP)

The invention provides an ammonia elimination reagent in solution, comprising a thermo-resistant isocitrate dehydrogenase with prominent stability under conditions at high alkaline pHs. For example, the isocitrate dehydrogenase is preferably derived from the genus Thermus. For an assay system of biological substances generating a reaction product ammonia, an ammonia elimination reagent can be prepared by selecting and using the enzyme; the resulting ammonia elimination reagent can be stored in solution; additionally, the assay system can be designed in combination with both the coenzymes NAD and NADP . The ammonia elimination reagent is novel and can eliminate ammonia in an extremely short time.

Ammonia elimination liquid reagent

The present invention provides a process for mass producing recombinant, thermostable GLDH at a low cost. The invention also provides a process for mass producing recombinant, thermostable GLDH at a low cost, by culturing a transformant without using a drug such as IPTG. The invention further provides thermostable GLDH which can use more stable NADH as a coenzyme in an ammonia assay reagent.

Thermostable glutamate dehydrogenase and process for producing the same

The present invention provides a gene encoding the type B subunit protein of avian lactate dehydrogenase. The gene encoding the type B subunit protein of avian lactate dehydrogenase of the present invention is obtained by plaque hybridization or the like from a cDNA library derived from avian heart muscle and encodes the type B subunit protein of avian lactate dehydrogenase having an amino acid sequence shown as SEQ ID NO. 2.

DNA encoding the subunit of avian lactate dehydrogenase

The present invention relates to a hexokinase that is stable in solution whether in the presence or the absence of glucose. The present enzyme is obtained from a culture of the thermophilic yeast, Kluyveromyces. It can be used for determination of ATP and glucose, and for determination of a biological component which produces ATP or glucose (e.g. creatine kinase).

Hexokinase obtained from thermophilic yeast Kluyveromyces fragilis

The invention relates to an ammonia elimination reagent for use in an enzymatic assay of a biological substance which produces ammonia as the reaction product. The reagent is an alkaline solution of pH 9 to 11 and contains Sulfolobus-derived thermostable isocitrate dehydrogenase, 2-oxoglutaric acid, a reducing coenzyme, isocitric acid, glutamate dehydrogenase, and a divalent metal salt. The reagent can be stored in solution and has excellent stability under conditions of alkaline pHs.

Alkaline reagent solution for eliminating ammonia in an assay

The present invention provides a gene encoding the type B subunit protein of avian lactate dehydrogenase. The gene encoding the type B subunit protein of avian lactate dehydrogenase of the present invention is obtained by plaque hybridization or the like from a cDNA library derived from avian heart muscle and encodes the type B subunit protein of avian lactate dehydrogenase having the sequences shown as SEQ ID NO. 1 or 2.

GMT is produced by E. coli transformant with an expression vector having introduced therein cDNA of glycine-N-methyl transferase (GMT) derived from rat liver. This process can produce GMT of a high purity and a high activity on an industrial scale.

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Osaka-fu, Japan

Hirokazu Matsukawa