Toyo Boseki Kabushiki Kaisha

Toyo Boseki Kaubshiki Kaisha

Shigenori Emi

Yukihiro Sogabe

Kazumi Yamamoto

Atsushi Sogabe

Shizuo Hattori

Toshiro Kikuchi

Shinichi Teshima

Minoru Kamimura

Yoshio Kojima

Yoshihisa Kawamura

Yoshiaki Nishiya

Takahide Kishimoto

Masachika Takashio

Seiji Takeshima

Yukio Takii

Yuzuru Suzuki

Yuji Takamoto

Kohji Sugihara

Tatsuro Shigyo

Toshio Kurihara

Masanori Oka

Yoshihiro Soya

Tsuneo Hanyu

Makoto Ando

Hisao Yamamoto

Naoko Tanigaki

Kayoko Furukawa

Shinichi Teschima

Michiyo Minami

Toshiyuki Nishio

Yoshihiro Yamamoto

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

This invention relates to DNA containing a gene encoding uricase, a plasmid having said DNA, a transformant containing said plasmid, and a process for producing uricase by using said transformant.

DNA sequence for uricase and manufacturing process of uricase

A protein having an .alpha.-glucosidase activity, wherein its N-terminal amino acid sequence is the sequence depicted in the Sequence Listing of the present invention at Sequence No. 1; a DNA having the genetic information of the protein having an .alpha.-glucosidase activity; a recombinant vector containing said DNA; a transformant transformed with said vector; and production of .alpha.-glucosidase comprising culture of said transformant in a medium so as to grow .alpha.-glucosidase, and harvesting said .alpha.-glucosidase. According to the present invention, .alpha.-glucosidase without contamination of amylase can be easily produced in high yields and in large amounts by genetic engineering.

Protein having .alpha.-glucosidase activity, DNA having genetic

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

The sorbitol oxidase of the present invention catalyzes the reaction in which D-sorbitol is oxidized D-glucose and hydrogen peroxide.

Sorbitol oxidase reagent from xanthomonas

This invention relates to an isolated uricase which is stable in an aqueous solution at a temperature up to 60.degree. C. and at a pH of 8.0 for 10 minutes.

Isolated recombinant uricase

A DNA fragment that contains a gene encoding creatinine amidohydrolase is provided. This invention also provides a recombinant vector containing the said DNA fragment, a transformant containing the said vector, and a method for producing creatinine amidohydrolase by the use of the said transformant.

DNA fragment containing a gene encoding creatinine amidohydrolase

A method for measuring carbon dioxide, comprising the steps of: (1) reacting bicarbonate ion in a sample with phosphoenolpyruvate carboxylase derived from an acetic acid bacterium in the presence of phosphoenolpyruvate; (2) reacting the resultant oxalacetic acid with malate dehydrogenase in the presence of NADH; and (3) measuring decreased NADH, and a reagent for measuring carbon dioxide, comprising phosphoenolpyruvate, phosphoenolpyruvate carboxylase derived from an acetic acid bacterium, malate dehydrogenase, NADH and a buffer. According to the present invention, a highly stable reagent for CO.sub.2 measurement, which permits a long-term storage in a liquid state, can be provided by the use of phosphoenolpyruvate carboxylase derived from a species of acetic acid bacteria.

Method for measuring carbon dioxide and reagent therefor

A method for determining .alpha.-amylase activity which involves bringing a sample into contact with an .alpha.-glucosidase in the presence of an .alpha.-amylase substrate and optically determining a liberated label, the substrate being a maltooligosaccharide composed of at least 3 glucose units, whose reducing terminal glucose is bonded to an optically measurable label at the 1-position by .alpha.-glucoside linkage or .beta.-glucoside linkage, and whose non-reducing terminal glucose is modified by a substituent other than glucose, and the .alpha.-glucosidase being substantially capable of acting on glucose to which the label is bonded at the 1-position by .alpha.-glucoside linkage and on all maltooligosaccharides having 2 to 7 glucose units; and a reagent for determining .alpha.-amylase activity comprising the .alpha.-glucosidase and said .alpha.-amylase substrate. The present invention permits, in the determination of .alpha.-amylase activity, efficient auxiliary action of adjuvant enzyme, a determination with good sensitivity, and little reagent blank reaction.

Method for determination of .alpha.-amylase activity

A protein having an .alpha.-glucosidase activity, wherein its N-terminal amino acid sequence is the sequence depicted in the Sequence Listing of the present invention at Sequence No: 1; a DNA having the genetic information of the protein having an .alpha.-glucosidase activity; a recombinant vector containing said DNA; a transformant transformed with said vector; and production of .alpha.-glucosidase comprising culture of said transformant in a medium so as to grow .alpha.-glucosidase, and harvesting said .alpha.-glucosidase. According to the present invention, .alpha.-glucosidase without contamination of amylase can be easily produced in high yields and in large amounts by genetic engineering.

DNA encoding .alpha.-glucosidase and method of producing same by genetic

A method for measuring carbon dioxide, comprising the steps of: (1) reacting bicarbonate ion in a sample with phosphoenolpyruvate carboxylase derived from an acetic acid bacterium in the presence of phosphoenolpyruvate; (2) reacting the resultant oxalacetic acid with malate dehydrogenase in the presence of NADH; and (3) measuring decreased NADH, and a reagent for measuring carbon dioxide, comprising phosphoenolpyruvate, phosphoenolpyruvate carboxylase derived from an acetic acid bacterium, malate dehydrogenase, NADH and a buffer. According to the present invention, a highly stable reagent for CO.sub.2 measurement, permitting a long-term storage in a liquid state can be provided by the use of phosphoenolpyruvate carboxylase derived from an acetic acid bacterium.

An isolated sorbitol oxidase from Xanthomonas maltophilia FERM BP-4512 is disclosed. The oxidase catalyzes the reaction of D-sorbitol+O.sub.2 .fwdarw.D-glucose+H.sub.2 O.sub.2, has a substrate specificity for D-sorbitol, D-mannitol, D-xylitol, and D-arabitol, has an optimum pH of 6.5 to 7.5, and has a molecular weight of 54 kD as determined by gel filtration or 43 kD as determined by SDS-PAGE. The enzyme can be used for measuring a polyol in a sample and as a reagent in a kit used for determining the presence of D-sorbitol.

Sorbitol oxidase from Xanthomonas maltophilia FERM BP-4512

There is disclosed a composition for measurement of potassium ion concentration, which contains a) pyruvate kinase, b) glycerol kinase, c) glycerol-3-phosphate oxidase, d) peroxidase, e) a chromogen of reduced type, f) adenosine diphosphate or a salt thereof, and g) phosphoenolpyruvic acid or a salt thereof. Also disclosed is a composition for elimination of ammonium ions, which contains a) glutamate dehydrogenase, b) glucose dehydrogenase, and c) nicotinamide adenine dinucleotide of reduced type (NADH) or nicotinamide adenine dinucleotide phosphate of reduced type (NADPH).

Composition for measurement of potassium ion concentration and

A substantially purified glucose dehydrogenase is disclosed. The enzyme has activity at a temperature of from about 30.degree. C. to about 65.degree. C. at a pH of from about pH 6 to about pH 10 and has an optimum activity at a temperature from about 50.degree. C. to about 60.degree. C. at a pH of from about 8.5 to about 9.0. The enzyme is further characterized by retaining at least 90% residual activity after treatment at 50.degree. C. for 15 minutes, being NAD or NADP dependent, having a molecular weight of about 101,000 daltons as determined by gel filtration using TSK gel, having an isoelectric point of about 4.5 by ampholyte isoelectric focusing, and having a specificity for at least .beta.-D-glucose and 2-deoxyglucose. The preferred source of the enzyme is Pseudomonas sp. FH1227.

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Tsuruga, Japan

Shigenori Emi