Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

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

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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.

Abstract: 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).

Abstract: 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.

Abstract: A new thermostable xanthine oxidase obtained from a microbe belonging to the genus Arthrobacter and a method of its production are disclosed. The present invention affords a xanthine oxidase which is excellent in thermal stability and which retains at least 70% residual activity after heat treatment at 60.degree. C. for 30 minutes. Arthrobacter luteus ATCC 21606 is the preferred microbe. The enzyme has a molecular weight of about 160,000 daltons as determined by gel filtration and a pH optimum of about 7.5.

Abstract: A pyruvate oxidase with excellent thermal stability, which is stable at pH 7.0 for 10 minutes at a temperature of up to 45.degree. C., an analytical method using said pyruvate oxidase, and an analytical reagent used for said method.

Abstract: .alpha.-glycerophosphate oxidase is produced by cultivating microorganisms belonging to genus Pediococcus, Streptococcus, Lactobacillus or Leuconostoc in a nutrient medium containing at least one compound selected from the group consisting of .alpha.-keto acids represented by the formula,R--COCOOHwherein R is CH.sub.3 (CH.sub.2).sub.m --, HOOC(CH.sub.2).sub.n -- or CH.sub.2 (OH)CH(OH)CH(OH)CH-- (in which m is an integer of 1 to 3 and n is an integer of 0 to 2) and salts thereof, and then .alpha.-glycerophosphate oxidase is recovered from the resulting culture broth. .alpha.-ketobutyric acid, .alpha.-ketovaleric acid, .alpha.-ketocaproic acid, .alpha.-ketomalonic acid, oxalacetic acid, .alpha.-ketoglutaric acid and .alpha.-ketogluconic acid are disclosed.