公开(公告)号：US4357425A

公开(公告)日：1982-11-02

申请号：US256901

申请日：1981-04-23

申请人： Eiichi Yoshino ,  Hidehiko Ishikawa ,  Fumitaka Inoue ,  Masaki Takada ,  Hideo Misaki

发明人： Eiichi Yoshino ,  Hidehiko Ishikawa ,  Fumitaka Inoue ,  Masaki Takada ,  Hideo Misaki

IPC分类号： C12N9/06 ,  C12R1/645

CPC分类号： C12N9/0022 ,  Y10S435/911

摘要： L-amino acid oxidase is obtained by culturing a microorganism which can produce L-amino acid oxidase and belongs to the genus Colletotrichum, e.g. Colletotrichum sp. M5073, deposition number FERMP 5441, in a culturing medium and recovering the oxidase from cells of the microorganism.

摘要翻译： 通过培养可产生L-氨基酸氧化酶并属于Colletotrichum属的微生物获得L-氨基酸氧化酶，例如， Colletotrichum sp。 M5073，沉积编号FERMP 5441，并在微生物的细胞中回收氧化酶。

公开(公告)号：US4346173A

公开(公告)日：1982-08-24

申请号：US201123

申请日：1980-10-27

申请人： Shigeru Ikuta ,  Shigeyuki Imamura ,  Hidehiko Ishikawa ,  Kazuo Matsuura ,  Masaki Takada ,  Hideo Misaki

发明人： Shigeru Ikuta ,  Shigeyuki Imamura ,  Hidehiko Ishikawa ,  Kazuo Matsuura ,  Masaki Takada ,  Hideo Misaki

IPC分类号： C12N9/02

CPC分类号： C12Y103/03006 ,  C12N9/001 ,  C12R1/06 ,  C12R1/645 ,  C12R1/66 ,  C12R1/865 ,  Y10S435/83 ,  Y10S435/911 ,  Y10S435/913 ,  Y10S435/942

摘要： A process for the production of acyl-Coenzyme A oxidase, comprises culturing an acyl-Coenzyme A-oxidase-producing microorganism belonging to genus Macrophomina, genus Cladosporium, genus Aspergillus, genus Monascus, genus Saccharomyces or genus Arthrobacter in a nutrient medium, and isolating the thus-formed acyl-CoA oxidase therefrom. The preferred species of microorganism are Macrophomina phaseoli ATCC 14383, Cladosporium resinae IFO 6367, Aspergillus candidus M-4815 FERM-P No. 5226, Monascus sp. M-4800 FERM-P No. 5225, Saccharomyces cerevisiae Y 0036 FERM-P No. 5174, and Arthrobacter sp. B-720 FERM-P No. 5224, respectively.

摘要翻译： 一种制备酰基辅酶A氧化酶的方法，包括在营养培养基中培养属于巨噬细胞，枝孢霉属，曲霉属，红曲霉属，酿酒酵母属或节杆菌属的酰基辅酶A氧化酶微生物， 由此形成的酰基辅酶A氧化酶。 微生物的优选种类是Macrophomina phaseoli ATCC 14383，Cladosporium resinae IFO 6367，Aspergillus candidus M-4815 FERM-P No.5226，Monascus sp。 M-4800 FERM-P No.5225，酿酒酵母Y 0036 FERM-P No.5174和节杆菌属（Arthrobacter sp。 B-720 FERM-P No. 5224。

公开(公告)号：US5206146A

公开(公告)日：1993-04-27

申请号：US481752

申请日：1990-02-15

申请人： Hideo Misaki ,  Hidehiko Ishikawa ,  Kazuo Matsuura

发明人： Hideo Misaki ,  Hidehiko Ishikawa ,  Kazuo Matsuura

IPC分类号： C12N9/00 ,  C12Q1/00 ,  C12Q1/25 ,  C12Q1/48 ,  C12Q1/50

CPC分类号： C12N9/93 ,  C12Q1/008 ,  C12Q1/25 ,  C12Q1/48 ,  C12Q1/50 ,  Y10S435/836

摘要： An assay method for a component in a specimen containing any one of ATP, deamide-NAD and an amide donor which comprises performing a main reaction which comprises incubating the specimen with NAD synthetase in the presence of ATP, deamide-NAD, an amide donor and Mg.sup.++ to generate NAD; performing a coenzyme cycling reaction by combining the oxidation-reduction reaction system with coenzyme NAD and the oxidation-reduction reaction system with coenzyme reduced NAD, and measuring a consumed or generated component in the cycling reaction. The NAD synthetase can be produced by culturing the microorganism Bacillus licheniformis B-0844 FERM P-6809, in a culture medium, and isolating the thus-produced NAD synthetase therefrom.

摘要翻译： 含有ATP，脱酰胺-NAA和酰胺供体中的任一种的样品中的组分的测定方法，其包括进行主要反应，其包括在ATP，脱酰胺-NAD，酰胺供体的存在下将样品与NAD合成酶孵育， Mg ++生成NAD; 通过将氧化还原反应体系与辅酶NAD和氧化还原反应体系与辅酶还原NAD进行组合进行辅酶循环反应，测定循环反应中消耗或产生的成分。 NAD合成酶可以通过在培养基中培养微生物地衣芽孢杆菌B-0844 FERM P-6809，并从其中分离由此产生的NAD合成酶来制备。

公开(公告)号：US4683198A

公开(公告)日：1987-07-28

申请号：US674009

申请日：1984-11-23

申请人： Hidehiko Ishikawa ,  Kazuo Matsuura ,  Hideo Misaki

发明人： Hidehiko Ishikawa ,  Kazuo Matsuura ,  Hideo Misaki

IPC分类号： C12N9/04 ,  C12Q1/32 ,  C12R1/44 ,  C12Q1/40

CPC分类号： C12N9/0006 ,  C12Q1/32 ,  Y10S435/882 ,  Y10S435/883 ,  Y10S435/884

摘要： An enzyme which acts on a reducing terminal of a monosaccharide or oligosaccharide without requiring NAD or NADP and which catalyzes the reaction ##STR1## wherein R is a saccharide chain residue or hydrogen, A is a hydrogen acceptor other than NAD or NADP, AH or AHn is a reduced form acceptor and n is 1 or 2. This maltose dehydrogenase is produced by culturing a microorganism belonging to genus Staphylococcus, specifically, sp. B-0875 FERM BP-385, and isolating the thus-produced maltose dehydrogenase from the culture medium. An assay method for the determination of saccharide or the activity of a saccharide liberating enzyme, comprises reacting this enzyme with a substrate in the presence of a hydrogen acceptor, and measuring the amount of a detectable change.

摘要翻译： 作用于单糖或寡糖的还原末端而不需要NAD或NADP并且催化反应的酶，其中R是糖链残基或氢，A是NAD以外的氢受体或 NADP，AH或AHn是还原型受体，n是1或2.这种麦芽糖脱氢酶是通过培养属于葡萄球菌属的微生物，特别是sp。 B-0875FERM BP-385，并从培养基中分离由此产生的麦芽糖脱氢酶。 用于测定糖类或糖释放酶活性的测定方法包括在氢受体存在下使该酶与底物反应，并测量可检测的变化量。

公开(公告)号：US4331763A

公开(公告)日：1982-05-25

申请号：US217178

申请日：1980-12-16

申请人： Eiji Matsumura ,  Hidehiko Ishikawa ,  Hideo Misaki

发明人： Eiji Matsumura ,  Hidehiko Ishikawa ,  Hideo Misaki

IPC分类号： C12N9/02 ,  C12N9/04

CPC分类号： C12Y110/03003 ,  C12N9/0063

摘要： Ascorbate oxidase is produced by extraction from plants of the genus Sechium, particularly the species thereof which is Sechium edule Sw. The crushed plant tissues are extracted with an aqueous alkaline solvent, preferably at about pH 11. The extract is then subjected to centrifugation, concentration under vacuum, salting out with ammonium sulfate and solvent fractionation with acetone, to prepare crude ascorbate oxidase, which is then further purified by dialysis, ion exchange chromatography, adsorption chromatography and gel filtration. The ascorbate oxidase thus obtained has an optimum pH of about 7, a km value of 0.3 mM, an isoelectric point of around pH 6.3 and a molecular weight of about 100,000.

摘要翻译： 抗坏血酸氧化酶通过从Sechium属植物中提取而产生，特别是Sechium edule Sw的种类。 粉碎的植物组织用碱性水溶液萃取，优选在约pH 11下。然后将提​​取物进行离心，在真空下浓缩，用硫酸铵盐析并用丙酮溶剂分级，制备粗抗坏血酸氧化酶 进一步通过透析，离子交换层析，吸附层析和凝胶过滤纯化。 由此获得的抗坏血酸氧化酶具有约7的最佳pH，0.3mM的km值，约6.3的等电点和约100,000的分子量。

公开(公告)号：US4427771A

公开(公告)日：1984-01-24

申请号：US311263

申请日：1981-10-14

申请人： Hideo Misaki ,  Eiji Muramatsu ,  Hidehiko Ishikawa ,  Kazuo Matsuura

发明人： Hideo Misaki ,  Eiji Muramatsu ,  Hidehiko Ishikawa ,  Kazuo Matsuura

IPC分类号： C12N9/04 ,  C12Q1/40 ,  C12N1/20 ,  C12Q1/32 ,  C12R1/11

CPC分类号： C12N9/0006 ,  C12Q1/40 ,  G01N2400/18 ,  Y10S435/837

摘要： An assay method for amylase activity in a biological specimen such as serum, saliva or urine. The enzyme amylase in the specimen is used to decompose a substrate which is a glucose polymer having a modified reducing terminal glucose residue or a cyclic glucose polymer. A component of the decomposed substrate is measured as an indication of amylase activity in the specimen. The residue may be amylose, amylopectin, starch, starch hydrolyzate, an etherified reducing terminal, an esterified reducing terminal, gluconolactone or a gluconic acid residue or its derivative. Decomposed substrate assay may be effected by contacting the same with maltose dehydrogenase and NAD or NADP, whereupon the assay is performed by measuring the amount of reduced NAD or reduced NADP, by reacting the same with reduced-form hydrogen transport colorimetric reaction reagent. This reagent may be a tetrazolium salt and diaphorase, or tetrazolium salt and phenazinemethosulfate. To remove pre-existing glucose and maltose present in the specimen, the specimen may be pretreated with alpha-glucosidase or kinase in the presence of Mg.sup.++ and ATP, the kinase being for example hexokinase. The preferred maltose dehydrogenase is produced by culturing Bacillus megaterium B-0779 FERM-P No. 5662.

摘要翻译： 生物样品如血清，唾液或尿液中淀粉酶活性的测定方法。 试样中的酶淀粉酶用于分解具有修饰的还原性末端葡萄糖残基或环状葡萄糖聚合物的葡萄糖聚合物的底物。 测量分解的底物的组分作为样品中淀粉酶活性的指示。 残基可以是直链淀粉，支链淀粉，淀粉，淀粉水解物，醚化还原末端，酯化还原末端，葡萄糖酸内酯或葡萄糖酸残基或其衍生物。 分解的底物测定可以通过使其与麦芽糖脱氢酶和NAD或NADP接触来实现，因此通过使其与还原形式的氢转运比色反应试剂反应来测量还原的NAD或还原的NADP的量来进行测定。 该试剂可以是四唑盐和心律黄素，或四唑鎓盐和吩嗪甲硫酸盐。 为了除去样品中存在的现有葡萄糖和麦芽糖，可以在Mg ++和ATP存在下用α-葡糖苷酶或激酶预处理样品，所述激酶例如己糖激酶。 优选的麦芽糖脱氢酶是通过培养巨大芽孢杆菌B-0779 FERM-P No.5662产生的。

公开(公告)号：US4767712A

公开(公告)日：1988-08-30

申请号：US603710

申请日：1984-04-25

申请人： Hideo Misaki ,  Hidehiko Ishikawa ,  Kazuo Matsuura

发明人： Hideo Misaki ,  Hidehiko Ishikawa ,  Kazuo Matsuura

IPC分类号： G01N33/50 ,  C12N9/00 ,  C12Q1/00 ,  C12Q1/25 ,  C12Q1/26 ,  C12Q1/48 ,  C12Q1/50 ,  C12R1/10 ,  C12N1/20

CPC分类号： C12N9/93 ,  C12Q1/008 ,  C12Q1/25 ,  C12Q1/48 ,  C12Q1/50 ,  Y10S435/836

摘要： An assay method for a component in a specimen containing any one of ATP, deamide-NAD and an amide donor which comprises performing a main reaction which comprises incubating the specimen with NAD synthetase in the presence of ATP, deamide-NAD, an amide donor and Mg.sup.++ to generate NAD; performing a coenzyme-cycling reeaction by combining the oxidation-reduction reaction system with coenzyme NAD and the oxidation-reduction reaction system with coenzyme reduced NAD, and measuring a consumed or generated component in the cycling reaction. The NAD synthetase can be produced by culturing the microorganism Bacillus licheniformis B-0844 FERM P-6809, in a culture medium, and isolating the thus-produced NAD synthetase therefrom.

摘要翻译： 含有ATP，脱酰胺-NAA和酰胺供体中的任一种的样品中的组分的测定方法，其包括进行主要反应，其包括在ATP，脱酰胺-NAD，酰胺供体的存在下将样品与NAD合成酶孵育， Mg ++生成NAD; 通过将氧化还原反应体系与辅酶NAD和氧化还原反应体系与辅酶还原NAD结合，进行辅酶循环反应，测定循环反应中消耗或产生的成分。 NAD合成酶可以通过在培养基中培养微生物地衣芽孢杆菌B-0844 FERM P-6809，并从其中分离由此产生的NAD合成酶来制备。

公开(公告)号：US4605615A

公开(公告)日：1986-08-12

申请号：US472174

申请日：1983-03-02

申请人： Hidehiko Ishikawa ,  Hideo Misaki ,  Naoki Muto

发明人： Hidehiko Ishikawa ,  Hideo Misaki ,  Naoki Muto

IPC分类号： C12N9/52 ,  C12N9/02 ,  C12N9/06 ,  C12Q1/26 ,  C12R1/465 ,  C12Q1/52 ,  C12Q1/36

CPC分类号： C12N9/0022 ,  C12Q1/26 ,  Y10S435/886

摘要： L-glutamic acid oxidase having the following biochemical properties:(a) substrate specificity: L-glutamic acid,(b) enzyme action: catalyzes a reaction which forms one mole of .alpha.-ketoglutaric acid, one mole of ammonia and one mole of hydrogen peroxide from one mole of L-glutamic acid, one mole of oxygen and one mole of water, as follows: ##STR1## This oxidase is produced by culturing microorganisms belonging to genus Streptomyces in a nutrient medium and isolating the thus-produced L-glutamic acid oxidase. Particular microorganisms of genus Streptomyces are sp. A7700 FERM P-6241 (NRRL No. 15267) and sp. 8063 FERM P-6242 (NRRL No. 15268). The oxidase can be used for detecting L-glutamic acid or L-glutamate, in an aqueous sample, because it catalyzes a reaction which forms one mole of .alpha.-ketoglutaric acid, one mole of ammonia and one mole of hydrogen peroxide from one mole of glutamic acid, one mole of oxygen and one mole of water. Thus, the consumed oxygen can be quantitatively determined, or the generated .alpha.-glutaric acid or ammonia or hydrogen peroxide can be quantitatively determined.

摘要翻译： 具有以下生物化学性质的L-谷氨酸氧化酶：（a）底物特异性：L-谷氨酸，（b）酶作用：催化形成1摩尔α-酮戊二酸，1摩尔氨和1摩尔氢的反应 1摩尔L-谷氨酸，1摩尔氧和1摩尔水的过氧化物如下：该氧化酶是通过在营养培养基中培养属于链霉菌属的微生物而产生的，并分离由此产生的 L-谷氨酸氧化酶。 链霉菌属的特殊微生物是sp。 A7700 FERM P-6241（NRRL No. 15267）和sp。 8063 FERM P-6242（NRRL No. 15268）。 氧化酶可用于检测水样品中的L-谷氨酸或L-谷氨酸，因为它催化反应，其形成1摩尔α-酮戊二酸，1摩尔氨和1摩尔过氧化氢从1摩尔 谷氨酸，1摩尔氧和1摩尔水。 因此，可以定量测定消耗的氧气，或者可以定量测定产生的α-戊二酸或氨或过氧化氢。

公开(公告)号：US4491631A

公开(公告)日：1985-01-01

申请号：US392010

申请日：1982-06-25

申请人： Shigeyuki Imamura ,  Hideo Misaki ,  Hidehiko Ishikawa ,  Kazuo Matsuura

发明人： Shigeyuki Imamura ,  Hideo Misaki ,  Hidehiko Ishikawa ,  Kazuo Matsuura

IPC分类号： C12N9/02 ,  C12N9/10 ,  C12N9/88 ,  C12Q1/25 ,  C12Q1/00 ,  C12N9/00 ,  C12N9/04 ,  C12Q1/26 ,  C12Q1/32 ,  C12Q1/42 ,  C12Q1/44 ,  C12Q1/46 ,  C12Q1/48 ,  C12Q1/60 ,  C12R1/38

CPC分类号： C12Y103/99003 ,  C12N9/001 ,  C12N9/1029 ,  C12N9/88 ,  C12Q1/25 ,  Y10S435/874

摘要： An enzyme having enoyl-CoA hydratase activity, 3-hydroxyacyl-CoA dehydrogenase activity and 3-ketoacyl-CoA thiolase activity, all in the same enzyme, is produced by culturing the microorganism strain Pseudomonas fragi B-0771 FERM-P No. 5701, and isolating the enzyme thus produced from the culture medium. Such an enzyme is useful in an assay method for a fatty acid component in a sample, which fatty acid is originally present in the sample or is liberated from a fatty acid ester in the sample, comprising:(a) converting the fatty acid to acyl-CoA;(b) converting the thus-produced acyl-CoA to dehydroacyl-CoA;(c) converting the thus-produced dehydroacyl-CoA to hydroxyacyl-CoA;(d) converting the thus-produced hydroxyacyl-CoA to ketoacyl-CoA;(e) converting the thus-produced ketoacyl-CoA to acyl-CoA; and measuring the detectable changes in the reaction mixture.A composition suitable for such lipid assay comprisesATP or GTP,CoASH,NAD,acyl-CoA synthetase activity,acyl-CoA oxidase activity,enoyl-CoA hydratase activity,3-hydroxyacyl-CoA dehydrogenase activity, and3-ketoacyl-CoA thiolase activity,wherein the last three activities are supplied by the new multi-active enzyme.

摘要翻译： 通过培养微生物菌株Pseudomonas fragi B-0771 FERM-P No. 5701制备具有烯酰辅酶A水合酶活性，3-羟基酰基-CoA脱氢酶活性和3-酮酰基-CoA硫羟酸酶活性的酶，全部在同一酶中， 并从培养基中分离由此产生的酶。 这样的酶可用于样品中的脂肪酸组分的测定方法，该脂肪酸最初存在于样品中或从样品中的脂肪酸酯中释放出来，其包括：（a）将脂肪酸转化为酰基 -CoA; （b）将由此产生的酰基辅酶A转化为脱氢酰基-CoA; （c）将由此产生的脱氢酰基-CoA转化为羟基酰基-CoA; （d）将由此产生的羟基酰基CoA转化为酮酰基-CoA; （e）将由此产生的酮酰基-CoA转化成酰基-CoA; 并测量反应混合物中可检测的变化。 适用于这种脂质测定的组合物包括ATP或GTP，CoASH，NAD，酰基-CoA合成酶活性，酰基-CoA氧化酶活性，烯酰辅酶A水合酶活性，3-羟基酰基-CoA脱氢酶活性和3-酮酰基-CoA硫解酶活性 其中最后三种活性由新的多活性酶提供。

公开(公告)号：US4182560A

公开(公告)日：1980-01-08

申请号：US895441

申请日：1978-04-11

申请人： Masanobu Oguchi ,  Hidehiko Ishikawa ,  Haruyoski Okuyama ,  Yasuo Uchida ,  Kiyoshi Izawa

发明人： Masanobu Oguchi ,  Hidehiko Ishikawa ,  Haruyoski Okuyama ,  Yasuo Uchida ,  Kiyoshi Izawa

IPC分类号： G03B17/24 ,  G03B27/73 ,  G03C5/02 ,  G03B27/32 ,  G03B27/76

CPC分类号： G03B27/73 ,  G03B17/24 ,  G03C5/02 ,  G03B2206/004 ,  G03B2217/243 ,  G03B2217/246

摘要： In a color printing method, a color photosensitive material is exposed in the photographing step to object illuminating light, which is recorded thereon as an optical density by photographic treatments. In the printing step, the optical density is detected to determine blue, green and red exposures, which cause the object illuminating light to be reproduced on a color positive photosensitive material so as to have neutral gray or to be colored to a standard color. An object image on the color photosensitive material is printed on the color positive photosensitive material with the most suitable color reproduction with the same three-color component exposures as those determined in printing the object illuminating light.

摘要翻译： 在彩色打印方法中，在拍摄步骤中曝光彩色感光材料，以照相光照射作为光密度记录在其上的照明光。 在打印步骤中，检测光密度以确定蓝色，绿色和红色曝光，这导致物体照明光在彩色正性感光材料上再现以具有中性灰色或被着色为标准颜色。 彩色感光材料上的物体图像被印刷在具有与打印物体照明光中确定的相同的三色成分曝光的最合适的颜色再现的彩色正性感光材料上。