Asahi Kasei Kogyo Kabushiki Kaisha

Toyo Jozo Kabushiki Kaisha

Toyo Jozo Company, Ltd.

Asahi Kasei Pharma Corporation

Mamoru Takahashi

Kazuo Matsuura

Hideo Misaki

Shigeyuki Imamura

Shigeru Ueda

Shigeru Ikuta

Shinobu Nagasawa

Masaki Takada

Hitoshi Sagai

Shinji Koga

Takashi Etoh

Keiko Nogata

Kimiko Hattori

Takuji Kozuma

Kouji Suzuki

A method for assaying ammonia and/or ammonium ions contained in a liquid sample which comprises subjecting the sample to a reaction at least in the presence of an NAD synthetase, deamidated NAD, ATP, Mg ions and/or Mn ions, a dehydrogenase capable of forming ammonia molecules from an amine substrate and an oxidized NAD, and the amine substrate, and then determining the amounts of the ingredients consumed or generated by the reaction; and an assaying composition comprising all of the above-specified ingredients. The method is inexpensive and is effective in accurately assaying ammonia and/or ammonium ions present in a few minutes.

Method for assaying ammonia using an NAD-based cycling reaction system

Highly sensitive method for assaying chiro-inositol and compositions for

Sorbitol kinase, process for producing the same, and substantially pure

Method and composition for quantitative determination of ammonia,

Method for the quantitative determination of D-3-hydroxybutyric acid and

A method of assaying for acyl-L-carnitines including short chain acyl-carnitines including acetyl-L-carnitine and propionyl-L-carnitine in a substance, comprises subjecting a sample of the substance to be analyzed to an enzymatic hydrolysis using an acyl-carnitine esterase. The esterase is produced by Alcaligenes sp. FERM BP-2570 and it has substrate specificity for acyl-L-carnitines including short-chain acyl-L-carnitines. In addition the esterase demonstrates substrate specificity for acetyl-L-carnitine and propionyl-L-carnitine. The enzyme facilitates the hydrolysis reaction of one mole each of the acyl-L-carnitines with one mole of water in which to form one mole each of the corresponding fatty acid and L-carnitine. The amount of the fatty acid and L-carnitine formed is determined by this method.

Method of assaying for acyl-L-carnitines and short-chain acyl-carnitines

Myo-inositol in a specimen is assayed by reacting a specimen containing myo-inositol with:

Highly sensitive assay method for myo-inositol, composition for

A method of assaying L-carnitine in a specimen comprises reacting a specimen containing L-carnitine with:

Highly sensitive assay method for L-carnitine and composition for

A new class of L-carnitine dehydrogenase is disclosed, which is stable in solution and has a residual activity of greater than 70% after one week in a pH 9.0 buffer solution at 5.degree. C., a molecular weight of 51,000.+-.6,000 daltons, a pH optimum of 9.0, a optimum temperature of 50.degree. C. and an isoelectric point of pH 5.3.+-.0.6. Also disclosed is a process for producing the new enzyme from a microorganism of the Alcaligenes genus, preferably the newly-discovered species Alcaligenes sp. No. 981 FERM BP-2570.

L-carnitine dehydrogenase from alcalgenes

An isolated L-carnitine dehydrogenase is disclosed, which is stable in solution and has a residual activity of greater than 70% after one week in a pH 9.0 buffer solution at 5.degree. C. Also disclosed is a process for producing the new enzyme from a microorganism of the Alcaligenes genus, preferably the newly-discovered species Alcaligenes sp. No. 981 FERM BP-2570.

L-carnitine dehydrogenase and process for its production

Glucose-6-phosphate dehydrogenase which is an enzyme for assaying creatinekinase for diagnolyzation of myocardial infraction is produced by culturing a transformant having DNA which codes amino acid sequence shown from its N-terminal in FIG. 1 and which is extraneous to a host to have genetic information of the DNA expressed and collecting glucose-6-phosphate dehydrogenase from the culture.

Gene and process of making glucose-6-phosphate dehydrogenase

Reagent for analysis of triglycerides contained in blood serum is provided, which comprises lipases and monoglyceride lipases capable of acting on monoglycerides having substrate specificity and capable of catalyzing the following enzymatic reaction: monoglyceride+H.sub.2 O.fwdarw.glycerol+fatty acids. The glycerol or fatty acids are measured to learn an amount of the triglycerides or fatty acid by any known analytical method.

Reagent for analysis of triglycerides and analysis using the same

A process for the production of L-alanine dehydrogenase which comprises culturing an L-alanine dehydrogenase producing microorganism belonging to the genus Sporolactobacillus in a nutrient medium and isolating thus-produced L-alanine dehydrogenase from the cultured mass. The microorganism is for example Sporolactobacillus sp. 78-3 FERM BP-2517 and mutants and variants thereof having the ability to produce L-alanine dehydrogenase in recoverable amounts. This strain is a thermophile which cannot grow at 40.degree. C. but can grow at 45.degree. C. and 52.degree. C. The strain can assimilate glucose and produce lactic acid and acetic acid.

Process for the production of L-alanine dehydrogenase from 78-3 FERM

Disclosed herein is a novel monoglyceride lipase at least capable of catalyzing an enzymatic reaction of the following equation (a) and as substrate specificity, capable of acting on monoglyceride but incapable of acting on diglyceride and triglyceride:

Novel monoglyceride lipase and its production process.

A novel bilirubin oxidase is provided having a substrate specificity for bilirubin but not to, at least, biliverdin, catechol and hemin and which catalyzes the enzyme reaction between two moles of bilirubin and one mole of oxygen to yield two moles of biliverdin and two moles of water. A process is also provided for the production of said novel bilirubin oxidase, which comprises cultivating a bilirubin oxidase-producing fungus of the genus Penicillium in a culture medium and collecting the bilirubin oxidase from the culture mixture. A method of determining the content of bilirubin in a sample to be analyzed is further provided which comprises contacting the sample with the bilirubin oxidase to convert bilirubin in the sample into biliverdin and determining the amount of biliverdin formed or the amount of oxygen consumed therefor, as well as a method for removing bilirubin contained in a sample to be analyzed, which comprises contacting the sample with said novel bilirubin oxidase.

Growing community of inventors

Shizuoka, Japan

Mamoru Takahashi