Abstract: The present invention aims at providing a reagent and a method for simply, rapidly, and accurately diagnosing renal dysfunction. According to the present invention, free ATP in a urine sample from a patient suffering from renal dysfunction is determined by a bioluminescent technique using luciferin and luciferase. By determining the value, it is possible to simply, rapidly, and accurately diagnose common renal dysfunction. Moreover, according to the present invention, it is possible to avoid renal dysfunction caused by side-effects of drugs, by collecting daily the urine of a patient who has been administered with carcinostatic that is toxic to kidney such as cisplatin or methotrexate, and analyzing the changes in the ATP level in the urine sample by a bioluminescent technique, thereby detecting hypersensitivity of the patient caused by such drug or by an excessive administration of such drug, or thereby determining an optimal dose (a maximum acceptable dose) of such drug.

Abstract: A method for analyzing an intracellular component comprising the following steps, and a reagent kit comprising (a) an extraction reagent, (b) branched dextrin or a derivative thereof, and (c) a reagent for analyzing an intracellular component: (1) step of adding an extraction reagent to a sample containing cells to extract the intracellular component; (2) step of adding branched dextrin or a derivative thereof to the sample containing the extraction reagent; and (3) step of analyzing the extracted intracellular component.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.