Toyo Jozo Kabushiki Kaisha

Toyo Jozo Company, Ltd.

Asahi Kasei Kogyo Kabushiki Kaisha

Nemoto & Company, Ltd.

Toyo Yozo Company, Ltd.

Hideo Misaki

Kazuo Matsuura

Shigeyuki Imamura

Hidehiko Ishikawa

Shigeru Ueda

Mamoru Takahashi

Shigeru Ikuta

Naoki Muto

Yoshifumi Horiuchi

Saburo Harada

Eiichi Yoshino

Masaki Takada

Kazuhiro Watanabe

Takashi Matsuzawa

Masahiko Taniuchi

Hirao Nagae

Yuzo Ishikawa

Masashi Tanno

Satoshi Takenaka

Mamoru Takahasi

Fumitaka Inoue

Tohru Matsumoto

Eiji Matsumura

Tsutomu Yamaguchi

Eiji Muramatsu

Method and composition for quantitative determination of ammonia,

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

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 for a high-sensitivity quantitative analysis of bile acid in a bile acid-containing sample utilizes a reagent comprising:

Method of high-sensitive analysis of bile acid and reagent composition

An assay method for a component in a specimen containing any one of ATP, deamide-NAD and an amide donor which comprises performing a main reaction which comprises incubating the specimen with NAD synthetase in the presence of ATP, deamide-NAD, an amide donor and Mg.sup.++ to generate NAD; performing a coenzyme cycling reaction by combining the oxidation-reduction reaction system with coenzyme NAD and the oxidation-reduction reaction system with coenzyme reduced NAD, and measuring a consumed or generated component in the cycling reaction. The NAD synthetase can be produced by culturing the microorganism Bacillus licheniformis B-0844 FERM P-6809, in a culture medium, and isolating the thus-produced NAD synthetase therefrom.

Assay method using NAD synthetase

Disclosed herein is a novel monoglygeride 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:

Analytical method making use of monoglyceride lipase

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

An assay with high sensitivity for activity of lecithin-cholesterol acyltransferase in blood for functional analysis of liver, by bringing the blood into contact with lecithin and free cholesterol until lysolecithin and cholesterol ester are produced, allowing the lysolecithin produced to react with lysophospholipase and glycerophosphocholine phosphodiesterase and assaying glycerol-3-phosphate produced simultaneously or successively in the reaction by means of an enzymatic cycling reaction in which glycerol-3-phosphate, dihydroxyacetone-3-phosphate, nicotinamide adenine dinucleotide (NAD), reduced NAD, O.sub.2, H.sub.2 O.sub.2, glycerophosphate oxidase and glycerophosphate dehydrogenase take part.

Assay method for lecithin-cholesterol acyltransferase

A colony counting apparatus includes a reading unit with a visual sensor incorporated therein. The presence of a colony is detected at the end of that colony by moving the reading unit along lines selected at an appropriate pitch and by reading data on the individual points set along each line as logical high or low signals. The values obtained in the above-described counting operation are added and stored in an addition/storage device in a CPU, and the results of addition which are stored in the addition/storage device are output to a suitable display by an outputting device when the counting operation is completed.

Colony counting apparatus

Ethanolamine in a sample can be assayed by treating the sample with ethanolamine oxidase, thereby to catalyze a reaction-consuming ethanolamine, oxygen and water, and forming glycolaldehyde, ammonia and hydrogen peroxide. The amount of consumed oxygen or the amount of generated ammonia or hydrogen peroxide is then determined, as a measure of the ethanolamine that was originally the sample. The ethanolamine can appear in the sample as such, or can be liberated simultaneously with or prior to the catalysis reaction, from an ethanolamine derivative, e.g. phosphatidyl ethanolamine by the action of phospholipase D. Ethanolamine oxidase can be produced from Bacillus sp. B-0783 FERM-P No. 5798 in a conventional culture medium, preferably by submerged aeration liquid culturation.

Assay method for phosphatidyl ethanolamine

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 NAD synthetase is produced by culturing a broth of Bacillus stearothermophilus H-804 FERM BP-1408. This new enzyme selectively catalyzes the reaction ##STR1## without catalyzing the reaction ##STR2## The enzyme uses ammonia or ammonium ion as a substrate, but does not use either glutamine or asparagine. Also disclosed is an assay method using the enzyme, for any one of ATP, deamide-NAD, ammonia or ammonium ion in a specimen to be assayed.

Novel NAD synthetase, assay method using said novel NAD synthetase and a

A composition and method for lipase assay, comprising the use of an aqueous solution of a 1,2-diglyceride of a higher fatty acid, and a nonionic surface active agent. The higher fatty acid is a higher fatty acid of 8 or more and preferably 12 or more carbons, most preferably a higher unsaturated fatty acid of more than 16 carbons. The concentration of 1,2-diglyceride is more than 0.5 g per liter of solution. The nonionic surface active agent is a polyoxyethylene-type nonionic surface active agent, a polyhydric-alcohol-type nonionic surface active agent or a block-polymer-type nonionic surface active agent, whose concentration is more than 0.1% by weight in the composition and which has an HLB more than 10. The composition preferably contains 0.5-10 g of 1,2-diglyceride and 10-50 g of nonionic surface active agent per liter of solution.

Composition for lipase assay

A highly sensitive quantitative assay method for a component which is 3.beta.-hydroxysteroid or 3-ketosteroid, in a specimen to be assayed, comprising causing this component in the specimen to take part in the cycling reaction ##STR1## and measuring a detectable change in the reaction system. There is thus provided a 3.beta.-hydroxysteroid - 3-ketosteroid cycling reaction using 3.beta.-hydroxysteroid oxidase, which consumes O.sub.2 and generates H.sub.2 O.sub.2 and 3-ketosteroid, with a substrate of 3.beta.-hydroxysteroid, or 3.beta.-hydroxysteroid dehydrogenase, which consumes reduced NAD(P) and generate NAD(P) and 3.beta.-hydroxysteroid, with a substrate of 3-ketosteroid. Example of specimens are specimens which contain 3-hydroxysteroid or 3-ketosteroid, or which liberate or generate such a component. By proceeding at a rate of more than ten cycles per minute and measuring the amount of a detectable change in the reaction, the component in a specimen can easily and sensitively be detected with good accuracy.

Growing community of inventors

Shizuoka, Japan

Hideo Misaki