Toyo Boseki Kabushiki Kaisha

Other

Yoshitomi Pharmaceutical Industries, Ltd.

Shinichi Teshima

Yoshihisa Kawamura

Kazumi Yamamoto

Shizuo Hattori

Shigenori Emi

Atsushi Sogabe

Seiji Takeshima

Yuzo Hayashi

Kazuko Matsumoto

Kazuhiro Matsui

Katsunori Ikeda

Noriyuki Hongo

Akira Shimada

Toshio Kurihara

Minoru Kamimura

Tsuneo Hanyu

Noboru Mitsuhida

Hisao Yamamoto

Katsutoshi Ishimaru

Yoshitaka Nakagiri

Toshiyuki Nishio

Insitu assay of substance in biological sample using labeled probe

Assay of substance in biological sample using labeled probe

A sugar ester derivative of the general formula (I) ##STR1## wherein G stands for a group of the formula (A) ##STR2## or a group of the formula (B) ##STR3## wherein .lambda. means 0 or 1; at least one of R.sub.1 and R.sub.2 means an ester residue of a saturated or unsaturated fatty acid having 1-30 carbon atoms and the other group means hydrogen atom or acetyl group, and R.sub.3 means a group of the formula (C) ##STR4## wherein X means a halogen atom, m means an integer of 0 to 4, Y means hydroxy group, an alkoxy group, a carboxyl group or sulfonic acid group, n means 0 or 1 and Z means nitro group or nitrovinyl group and its use. The sugar ester derivative of the general formula (I) is useful as a substrate for the measurement of lipase or esterase activities, and the reagents and the methods for measuring lipase or esterase activities which comprise said sugar ester derivative as the substrate are excellent in terms of reproducibility and sensitivity and enable the measurement of lipase or esterase activities in accordance with rate-assay method by an easy procedure.

Sugar ester derivatives, reagents for measurement of hydrolase activity

A novel glutamate dehydrogenase derived from the genus Pseudomonas which is specific to L-glutamic acid, requires NAD.sup.+ and NADH as coenzymes, does not act on NADP.sup.+ and NADPH, is with an optimum pH 10.5-11.5 (oxidative deamination), a pH stability of 5-10 (at 25.degree. C.; 20 hours), an optimum temperature of about 60.degree. C. (oxidative deamination) and a molecular weight of about 280,000 (gel filtration) or about 41,000 (SDS-PAGE) and is not activated by ADP. A reagent composition for measuring an amount of ammonia characterized in containing a glutamate dehydrogenase which is not activated by ADP and is NADH-dependent, .alpha.-ketoglutaric acid or a salt thereof and NADH; and a reagent composition wherein urease or creatinine deiminase is further added to the above-mentioned reagent composition.

Reagent composition of glutamate dehydrogenase from pseudomonas

A novel alkaline phosphatase and a method for the production of the alkaline phosphatase are described. A method for detecting a ligand in a sample and a method for analyzing the sequence of nucleic acid in a sample using the alkaline phosphatase are also described.

Alkaline phosphatase

Method and reagent for detecting a ligand in a sample

A novel glutamate dehydrogenase is derived from the genus Pseudomonas and is specific to L-glutamic acid, requires NAD.sup.+ and NADH as coenzymes, does not act on NADP.sup.+ and NADPH, has an optimum pH 10.5-11.5 (oxidative deamination), a pH stability of 5-10 (at 25.degree. C.; 20 hours), an optimum temperature of about 60.degree. C. (oxidative deamination) and a molecular weight of about 280,000 (gel filtration) or about 41,000 (SDS-PAGE) and is not activated by ADP.

Glutamate dehydrogenase from Pseudomonas

A novel protein having a heat-resistant malate dehydrogenase activity, a DNA fragment having a gene encoding said protein, a recombinant vector having said DNA fragment, a transformant transformed with said vector, a method for producing the protein having heat-resistant malate dehydrogenase activity by the use of said transformant, a reagent for GOT determination, comprising the above-mentioned novel protein having a heat-resistant malate dehydrogenase activity and a method for determining GOT activity, which comprises the use of said reagent. According to the present invention, a protein having a heat-resistant malate dehydrogenase activity and having higher purity and superior heat stability can be obtained. In addition, a reagent for GOT determination which is superior in long-term storage can be prepared by the use of the protein having a heat-resistant malate dehydrogenase activity.

Protein having heat-resistant malate dehydrogenase activity

Maltooligosaccharide derivatives represented by the general formula: ##STR1## wherein at least one of R.sup.1 and R.sup.2 denotes a radical represented by: R.sup.3 --S(O).sub.m --R.sup.4 or R.sup.3 --CO--R.sup.4, and the rest of them denotes hydrogen atom, an alkyl radical containing 1 to 6 carbon atoms or a phenyl radical, in which R.sup.3 is an alkyl radical containing 1 to 5 carbon atoms, R.sup.4 is an alkylene radical containing 1 to 5 carbon atoms, and m is 1 or 2, R.sup.5 denotes a substituted or non-substituted phenyl radical, and n denotes an integer of 1 to 8; and reagents comprising the maltooligosaccharide derivatives.

Maltooligosaccharide derivatives and reagents for determination of

A reagent for the determination of acid phosphatase in body fluids which contains as a substrate a compound of the formula: ##STR1## wherein X is a halogen atom, and n and m are each an integer of 1 to 4, and a method for the determination of acid phosphatase in body fluids using the reagent. The reagent is clinically useful for diagnosis of prostate diseases such as prostate carcinoma and prostatomegaly and observation of progress thereof.

Reagent for determination of acid phosphatase

There is provided an improved quantitative analysis for the determination of a substrate or enzyme. In the analysis for the enzyme, it is reacted with a known substrate and in the analysis for the substrate, it is reacted with a known enzyme and then the resultant substance is reacted with an oxidase to produce hydrogen peroxide which is then reacted with a peroxidase, phenol derivatie and coupler to form a colored material which is then subjected to colorimetic analysis. The improvement resides in conducting the foregoing process by adding to the test sample a first reagent containing the oxidase, peroxidase and phenol derivative represented by the formula: ##STR1## wherein R.sub.1 is .circle.a a lower alkyl group having one to five carbon atoms or .circle.b the group defined in .circle.a above having a hydroxyl or sulfonic acid group, R.sub.2 is a hydrogen or halogen atom, a lower alkyl group having one to five carbon atoms, a lower acyl group having one to five carbon atoms, a lower alkylether group having one to five carbon atoms, or a lower alkoxycarbonyl group having one to five carbon atoms, said groups being unsubstituted or substituted with a hydroxyl or sulfonic acid group, and n is 0 to 4. Then, there is added to the above mixture a second reagent containing the coupler and the enzyme.

Method for the determination of substrates or enzyme activities

Growing community of inventors

Tsuruga, Japan

Shinichi Teshima