Abstract: An object of the present invention is to provide a therapeutic agent for pulmonary fibrosis which has high therapeutic effect. The invention provides a therapeutic agent for pulmonary fibrosis which comprises, as an active ingredient, a compound represented by the following formula (I): wherein R represents a linear or branched alkyl group having 1 to 30 carbon atoms, a linear or branched alkenyl group having 2 to 30 carbon atoms, or a linear or branched alkynyl group having 2 to 30 carbon atoms, which may contain a cycloalkane or aromatic ring; X and Y each independently represent an oxygen atom or a methylene group, provide that X and Y do not simultaneously represent a methylene group; and M represents a hydrogen atom or an alkali metal atom.

Abstract: It is an object of the present invention to provide a method for easily producing sodium cyclic phosphatidic acid that can be used as food and drink. According to the present invention, provided is a method for producing sodium cyclic phosphatidic acid, comprising a step of allowing a lyso-type phospholipid to react with phospholipase D in the presence of sodium salts in an aqueous medium, and a step of recovering a precipitate or an upper layer liquid that is generated as a result of addition of ethyl alcohol to the obtained reaction solution.

Abstract: The present invention provides a method for producing a composition containing 2-acyl-lysophosphatidylserine, including (a) a step of obtaining a composition containing phosphatidylserine by allowing phospholipase D to act on a raw material containing phosphatidylcholine in the presence of serine and (b) a step of obtaining a composition containing 2-acyl-lysophosphatidylserine by allowing phospholipase A1 to act on the composition containing phosphatidylserine in the presence of one or more additives selected from the group consisting of the following (I), (II), and (III), in which (I) one or more salts selected from the group consisting of sulfate salts, phosphate salts, nitrate salts, citrate salts, and tartarate salts of monovalent cations, (II) a gum, and (III) an emulsifier.

Abstract: The present invention provides a method for producing a composition containing 2-acyl-lysophosphatidylserine, including (a) a step of obtaining a composition containing phosphatidylserine by allowing phospholipase D to act on a raw material containing phosphatidylcholine in the presence of serine and (b) a step of obtaining a composition containing 2-acyl-lysophosphatidylserine by allowing phospholipase A1 to act on the composition containing phosphatidylserine in the presence of one or more additives selected from the group consisting of the following (I), (II), and (III), in which (I) one or more salts selected from the group consisting of sulfate salts, phosphate salts, nitrate salts, citrate salts, and tartarate salts of monovalent cations, (II) a gum, and (III) an emulsifier.

Abstract: Compositions for accurately assaying a glycated protein by: 1) avoiding effects of globulin and ascorbic acid components, 2) stabilizing proteases and at least enzymes acting on glycated amino acids; 3) accurately assaying albumin; and 4) assaying glycated albumin while avoiding the effects of glycated hemoglobin, and an assay method are provided. Thus, the contents of a glycated protein and glycated albumin can be more accurately determined.

Abstract: Provided is a novel and useful method of measuring pyrophosphate in a sample. There may be provided a novel and useful method of measuring pyrophosphate in a sample using pyruvate orthophosphate dikinase, nicotinamide-nucleotide adenylyltransferase, and dehydrogenase.

Abstract: Composition for accurately assaying a glycated protein by: 1) avoiding effects of globulin and ascorbic acid components, 2) siabilizing proteases and at least enzymes acting on glycated amino acids; 3) accurately assaying albumin; and 4) assaying glycated albumin while avoiding the effects of glycated hemoglobin, and an assay method are provided. Thus, the contents of a glycated protein and glycated albumin can be more accurately determined.

Abstract: Compositions for accurately assaying a glycated protein by: 1) avoiding effects of globulin and ascorbic acid components, 2) stabilizing proteases and at least enzymes acting on glycated amino acids; 3) accurately assaying albumin; and 4) assaying glycated albumin while avoiding the effects of glycated hemoglobin, and an assay method are provided. Thus, the contents of a glycated protein and glycated albumin can be more accurately determined.

Abstract: Stabilizers for colorants used for detection of enzymatic reactions, having a cyclodextrin and a catalase; reagents including stabilizers; and methods of use of such stabilizers and reagents.

Abstract: Diglyceride solutions for lipase activity determination, comprising at least one diglyceride, a low concentration buffer, and a nonionic surfactant.

Abstract: Provided is a novel and useful method of measuring pyrophosphate in a sample. There may be provided a novel and useful method of measuring pyrophosphate in a sample using pyruvate orthophosphate dikinase, nicotinamide-nucleotide adenylyltransferase, and dehydrogenase.

Abstract: [PROBLEMS] To provide lipase activity determination reagents which function by an enzymatic method. The reagents are easy to use in an ordinary clinical examination, have excellent handleability, and are excellent in accuracy and reproducibility. [MEANS FOR SOLVING PROBLEMS] Lipase activity is determined with any of reagents which comprise a low-concentration buffer and a diglyceride dissolved therein. The diglyceride is used as a substrate for lipase, whereby the liquid reagents can have long-term storage stability. One of the reagents converts a monoglyceride yielded by a lipase reaction into glycerol with the aid of monoglyceride lipase, and further contains glycerol kinase, pyruvate kinase, lactate dehydrogenase, reduced NAD, ATP, and phosphoenol pyruvate.

Abstract: Provided are: a protease reaction promoter which is superior in usefulness to the known protease reaction promoters; a stabilizer for a colorant used for detection of an enzymatic reaction, and a method of stabilizing the colorant; and a reagent for and a method of measuring a glycated protein and a ratio of a glycated protein using the same.

Abstract: Compositions for accurately assaying a glycated protein by: 1) avoiding effects of globulin and ascorbic acid components, 2) siabilizing proteases and at least enzymes acting on glycated amino acids; 3) accurately assaying albumin; and 4) assaying glycated albumin while avoiding the effects of glycated hemoglobin, and an assay method are provided. Thus, the contents of a glycated protein and glycated albumin can be more accurately determined.

Abstract: Compositions for accurately assaying a glycated protein by: 1) avoiding effects of globulin and ascorbic acid components, 2) siabilizing proteases and at least enzymes acting on glycated amino acids; 3) accurately assaying albumin; and 4) assaying glycated albumin while avoiding the effects of glycated hemoglobin, and an assay method are provided. Thus, the contents of a glycated protein and glycated albumin can be more accurately determined.

Abstract: An enzyme immobilizing carrier is produced by dissolving low-molecular weight chitosan in an aqueous acid solution and dropping the solution into a basic solution to produce regenerated porous chitosan in particles, reacting the regenerated porous chitosan in particles with the glycidyl ether of an aliphatic polyalcohol, and reacting further the resulting chitosan with the acid halide or acid anhydride of a higher fatty acid in a polar organic solvent. An enzyme and a polyfunctional cross-linking agent are reacted with the carrier to covalently immobilize the enzyme on the carrier. In a preferred embodiment, the enzyme is lipase and the carrier is produced by introducing the glycidyl ether of an aliphatic polyalcohol at 0.01 to 0.4 mole to 1 mole of the pyranose ring residue of the chitosan and by introducing a higher fatty acid having a total carbon number of 6 to 20 at 0.05 to 1 mole to 1 mole of the pyranose ring residue of the chitosan.

Abstract: Myo-inositol in a specimen is assayed by reacting a specimen containing myo-inositol with:a) myo-inositol dehydrogenase using a thio-NADP group or thio-NAD group and an NADP group or NAD group as coenzymes, and which catalyzes a reversible reaction forming myo-inosose from myo-inositol,b ) A.sub.1 andc) B.sub.1to effect a cycling reaction ##STR1## wherein A.sub.1 is a thio-NADP group, thio-NAD group, NADP group or NAD group, A.sub.2 is a reduced form of A.sub.1, when A.sub.1 is a thio-NADP group or thio-NAD group, B.sub.1 is a reduced NADP group or reduced NAD group and when A.sub.1 is an NADP group or NAD group, B.sub.1 is a reduced thio-NADP group or reduced thio-NAD group, and wherein B.sub.2 is an oxidized form of B.sub.1. The change in the amount of A.sub.2 generated or B.sub.1 consumed by the cycling reaction is measured to perform the assay. A composition for performing the assay comprises the above myo-inositol dehydrogenase, as well as the above components A.sub.1 and B.sub.1.

Abstract: A novel .omega.-carboxyalcohol oxidase catalyzes at least one of the following reactions:R--CH.sub.2 OH+O.sub.2 .fwdarw.R--CHO+H.sub.2 O.sub.2 a)R--CHO+O.sub.2 +H.sub.2 O.fwdarw.R--COOH+H.sub.2 O.sub.2 b)wherein R is alkyl, alkenyl, .omega.-carboxyalkyl or .omega.-carboxyalkenyl. The enzyme has substrate specificity on at least 12-hydroxydodecanoic acid, 1-dodecanol, 1-decanol, 1-octanol and 1-hexanol, and has no substrate specificity on methanol, ethanol or glycerol. The enzyme does not require the presence of NAD or NADP for its use. Also disclosed is a process for producing the enzyme, an assay method for substrates of the enzyme, and a process for producing carboxylic acid employing the enzyme.

Abstract: A method for assaying aliphatic alcohol, aliphatic aldehyde or .omega.-carboxylic acid derivatives thereof, using a novel .omega.-carboxyalcohol oxidase which catalyzes at least one of the following reactions:a) R--CH.sub.2 OH+O.sub.2 .fwdarw.R--CHO+H.sub.2 O.sub.2b) R--CHO+O.sub.2 +H.sub.2 O.fwdarw.R--COOH+H.sub.2 O.sub.2wherein R is alkyl, alkenyl, .omega.-carboxyalkyl or .omega.-carboxyalkenyl. The enzyme has substrate specificity on at least 12-hydroxydodecanoic acid, 1-dodecanol, 1-decanol, 1-octanol and 1-hexanol, and has no substrate specificity on methanol, ethanol or glycerol. The enzyme does not require the presence of NAD or NADP for its use. Also disclosed is a process for producing the enzyme, an assay method for substrates of the enzyme, and a process for producing carboxylic acid employing the enzyme.

Abstract: A novel .omega.-carboxyalcohol oxidase catalyzes at least one of the following reactions:a) R--CH.sub.2 OH+O.sub.2 .fwdarw.R--CHO+H.sub.2 O.sub.2b) R--CHO+O.sub.2 +H.sub.2 O.fwdarw.R--COOH+H.sub.2 O.sub.2wherein R is alkyl, alkenyl, .omega.-carboxyalkyl or .omega.- carboxyalkenyl. The enzyme has substrate specificity on at least 12-hydroxydodecanoic acid, 1-dodecanol, 1-decanol, 1-octanol and 1-hexanol, and has no substrate specificity on methanol, ethanol or glycerol. The enzyme does not require the presence of NAD or NADP for its use. Also disclosed is a process for producing the enzyme, an assay method for substrates of the enzyme, and a process for producing carboxylic acid employing the enzyme.