Kikkoman Corporation

Toyo Soda Manufacturing Co., Ltd.

Kikkoman Shoyu Co., Ltd.

Motoo Nakajima

Seiji Murakami

Kazuhiro Imai

Kiyoshi Mizusawa

Noriaki Hattori

Tatsuya Sakakibara

Keiko Yajitate

Teruo Watarai

Yoshio Shirokane

Akio Tsuji

Naoki Eisaki

Kazumasa Aoyagi

Masako Maeda

Kenkiti Koiso

Kazuo Nakamura

Diagnostic reagents for renal function disorders and method for analyzing urine samples

Method for analyzing intracellular components

The present invention provides a process for eliminating effectively ATP in a sample, using adenosine phosphate deaminase alone or in combination with at least one enzyme from the group consisting of apyrase, alkaline phosphatase, acid phosphatase, hexokinase and adenosine triphosphatase, a process for determining biological cells contained in foods and beverages in convenient and precise manner in combination with bioluminescence method, and a reagent for the determination thereof.

ATP eliminator and the process for determining biological cells

The present invention provides a process for eliminating effectively ATP in a sample, using adenosine phosphate deaminase alone or in combination with at least one enzyme selected from the group consisting of apyrase, alkaline phosphatase, acid phosphatase, hexokinase and adenosine triphosphatase, a process for determining biological cells contained in foods and beverages in convenient and precise manner in combination with bioluminescence method, and a reagent for the determination thereof.

There is provided a bioluminescence reagent comprising at least pyruvate orthophosphate dikinase, phosphoenolpyruvic acid, pyrophosphoric acid, magnesium ion or another metallic ions, luciferin and luciferase, which reagent is such that the amount of luminescence is maintained in a high level and moreover stably without decaying for a long time in a bioluminescence reaction, and there is provided a method for quantitatively determining an adenosine phosphate ester or a substance taking part in the ATP conversion reaction in high sensitivity and high accuracy using an inexpensive and simple measuring apparatus.

Bioluminescent adenosine phosphate ester assay and reagent

The present invention is intended to provide an EIA method utilizing bioluminescence using a firefly luciferase. The EIA method of the present invention is characterized by using an ATP-generating enzyme as a labeling enzyme, subjecting ATP generated to bioluminescence by the use of the firefly luciferase, and measuring the quantity of light emitted. Acetate kinase is a preferred enzyme used in the method.

Enzyme immunoassay method employing acetate kinase

A separator (1; 51) including a solution reservoir (3; 53) having a solution chamber (3a; 53a) for putting therein a solution, a membrane support base (4; 54) joined to the solution reservoir, an ultrafiltration-oriented filtering membrane (5; 55) held between the solution reservoir and the support base, and a filtrate cup (2) attached to the support base, in which the solution reservoir and the support base are each respectively made of a thermoplastic material, wherein the solution reservoir is ultrasonically welded to the support base at a part (3b; 53b) thereof spaced apart by a predetermined distance (l.sub.1 ; l.sub.2) from the filtering membrane.

Centrifugal ultrafilter unit for ultrafiltration of biochemical solutions

In a method of formaldehyde determination by measuring the fluorescence of a fluorescent substance formed by the reaction of a formaldehyde-containing solution with a fluorescent reagent capable of forming said fluorescent substance by the reaction with formaldehyde, the improvement which comprises using as said fluorescence reagent a compound represented by the general formula CH.sub.3 C(NH.sub.2).dbd.CHCO.sub.2 R, wherein R represents an alkyl group having 1 to 4 carbon atoms.

Method for determination of formaldehyde

A monomethylamine-oxidizing enzyme can be obtained by cultivating in a medium a strain which belongs to Genus Bacillus and has an ability to produce a monomethylamine-oxidizing enzyme. This enzyme exhibits several beneficial properties including the ability to oxidatively deaminate the amino group of monomethylamine to produce formaldehyde, ammonia, and hydrogen peroxide. The enzyme exhibits a high substrate specificity for monomethylamine, ethylamine, and n-proplyamine while showing no substrate specificity for benzylamine, dimethylamine, trimethylamine, ethylenediamine and tryamine. In addition, the enzyme is stable through an elevated temperature range permitting faster reaction rates and therefore a shorter overall quantitative evaluation. Another property includes a low Km value which allows smaller quantities of the enzyme to be employed per sample.

Monomethylamine-oxidizing enzyme

In a method of formaldehyde determination by measuring the fluorescence of a fluorescent substance formed by allowing a formaldehyde-containing solution to react with a reagent capable of forming said fluorescent substance from formaldehyde, the improvement comprising measuring the fluorescence in the presence of a serum albumin.

A novel methylguanidine-decomposing enzyme can be obtained by cultivating in a medium a bacterium belonging to Genus Alcaligenes and having an ability to produce a methylguanidine-decomposing enzyme. This methylguanidine-decomposing enzyme has an ability to decompose methylguanidine into methylamine and urea. Its optimum pH range is 10.9-12.3 and its stable pH range is 5.0-10.6.

Growing community of inventors

Chiba, Japan

Motoo Nakajima