• 专利附录
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    • 专利摘要:
    1519134 Enzymatic determinations in the presence of ascorbate BOEHRINGER MANNHEIM GmbH 29 April 1977 [9 June 1976] 17993/77 Heading G1B Substrates or enzymes other than ascorbate oxidase are determined using a redox reaction as measurement reaction and in the presence of ascorbate oxidase to eliminate interference by ascorbate. Examples relate to determination of glucose, uric acid, glutamate, tyrosine (using 3- methyl-b-potassium sulphonyl-benzthiazolone-2 hydrazone (SMBTH) and tyrosinase), pyrocatechol (using SMBTH and diphenol oxidase), blood in urine (using solutions comprising (1) phosphoric acid trimorpholide; 2,5-dimethylhexane-2, 5-dihydroperoxide and ascorbate oxidase and (2) 3, 3', 5, 5'-tetramethylbenzidine and phenanthridine), blood in faeces.
    公开号:SU797592A3
    申请号:SU772481956
    申请日:1977-05-06
    公开日:1981-01-15
    发明作者:Даннингер Йозеф；Денеке Ульферт；Ланг Гунтер；Михал Герхард；Решлау Петер
    申请人:Берингер Маннхайм Гмбх (Фирма)；
    IPC主号:
    专利说明:

    (54) METHOD FOR DETERMINING SUBSTRATE OR ORGANIZING ACTIVITY IN BIOLOGICAL MATERIAL THAT 0.0057373 or 0.000573% ascorbate almost completely inhibits test to 41.5% cuvette 4 and 5 shows complete elimination of violation of these concentrations of ascorbate by addition of 0.0003 % ascorbate oxidase. PRI mme R 2. Detection of Gluco with 2,2, -azino-di (3-ethyl-benzthiazoline sulfonate (Sb)) iftSTS), ROTA and got) in a photometer, with a wavelength of 432, with a measurement temperature of 25 ° C (see tab. 2). The cuvette i corresponds to the undisturbed measurement (no ascorbate). Cuves 2 and 3 show that 0.000573% or 0.0000573. Mol.% ascorbate completely brake t test to 2.1%. Cells 4 and 5 show the complete elimination of the disturbance of these concentrations of ascorbate by the addition of 0.0003% ascorbate oxidase. Froze Detection of uric acid by means of phenol, amino-antipirin, POD and Uricae on an analytical machine (Auto Analyzar) Principle of tests for uric acid + -J- Oa + HaQ P allantoin + + HjOj - 2 H2.Og + 2,4-dichlorophenal + 4-aminoantipypyrin chinodic carrier + 2 HgO. Making solutions. Ascorb oxide reagent. The contents of vial 1 are dissolved in 600 bididistilled water. Additive 0.3 m Brij-35. The mixture is then cured in a dark vial at approximately four weeks, at one week. Reagent uricase. The contents of vial 2 are dissolved in 800 ml of bidistilled water. Additive 2.0 ml In g Ij-35. The mixture is then kept in a dark vial at approximately 4c for four weeks, at approximately 25 ° C for one week. Concentration of solutions. 0.63% phosphate buffered saline, pH 5.6. 0.35% Tris / Liquic acid, pH 8.9, uricase 0.001%, POD 0.000015%, 0.05% 2,4-dichlorophenol, 0.08% 4-aminoantipyrine. PRI me R 4. Detection of glucose with HK / Q 6P-OA, NADP, INT and diaphorase in the fortometer. The measured wavelength is 492 nm, the incubation temperature is 25 ° C (see Table 3). Cuvette 1 corresponds to the undisturbed dimension. Cuvette 2 shows that 0.0000573% ascorbate can inhibit the test by 34% cuvette 3 shows that 0.0003% ascorbate oxidase completely eliminates this violation. PRI me R 5. Determination of glutamate by means of diaphorase in the photometer. The measured wavelength is 492 nm, the temperature is 25 ° C (see Table 4}, Cuvette 1 corresponds to an undisturbed measurement. Cuvettes 2 and 3 show that 0.0029% or 0.00029% of ascorbate doesn’t brake 700% test or 100%. Cuvettes 4 and 5 show the complete elimination of this disorder by adding 0.00006% ascorbate oxidase. Example: Determination of tyrosine with 3-methyl-b potassium sulfonyl-benzthiazolone-hydra-zonome- (2) (SMBTH) and tyrosinase in a photometer measured The wavelength is 492 nm, the measured temperature is 25 ° C (see Table 5. Cuvette 1 corresponds to the undisturbed measurement; in cuvette 2, 0.0057% of ascorbate reduces the theoretical 35%, in cuvette 3, this violation is completely eliminated by the addition of 0.003% ascorbate oxidase. Example 7. Determination of pyrocatechin with SMBTH and diphenol oxidase (see Table 6). Cuvette 1 corresponds to the undisturbed measurement. In a cuvette, 20.01145% ascorbate reduces the theoretical value by 47%; this violation is completely eliminated in cuvette 3 with the addition of 0.0003% ascorbate oxidase.The resulting method allows to completely eliminate the errors caused by the presence of ascorbic acid during the redox reactions. Table 1
    Phosphate buffer solution, pH 7.01, 1,368%
    o-Dianisidine /, 0.5% POD, 0.18%
    Glucose solution, 0.172%
    Ascorbic Acid Solution
    Water
    Ascorbate oxidase 500 units / ml, 0.05%
    Incubation 1 min at reading E, then start reaction with
    GOD 0.0333% Incubation 30 min at & E Incubation 30 min with reading E ,, deE0.505 0,000
    Continued table. one
    0.03 0.03 0.030.030.03
    0.1 0.010.10.01
    0.12 0.02 0.11 -0.09
    -0.02. 0.02
    0.1 0.1 0.1 0.1 0.1, Read E, Calculate from & 0.541 0.010 0.316 0.540 0.543 calculation from AE 0.400.502 0.504
    Phosphate buffer solution, pH 7.5, 1.36%
    NADP INT by 0.1% Diaphorase 5 U / mp, 0.1% Glucose solution, 0.005% Ascorbate solution 0.17%
    Ascorbate Oxidase, 0.00035%
    Water
    Incubation 3 min at 25 s, reading E per 1 of reaction with HK / G6P-DH-pacTBop at 0.14% 0.050.05 0.05
    Incubation 15 min, reading E, calculation from Ej-E DE DE0.2340.307 0.230
    T a ti) and
    0.03
    0.04
    0.03
    Table 4 Reading IT-solution 0.2 Incubation 15 min at 25 s, reading
    LU
    Components
    Phosphate buffer solution pH 5.2, 3.4%
    SMBTH 0.1 mol, 3%
    Ascorbic acid solution. Oh, 112%
    Water
    Ascorbate Oxidase 500, 05%
    Tyrosinase, 0.2 Incubation 1 min at 0.036% tyrosine Incubation 1 hour at DE
    Continued table. four
    0.184 1.560 0.380 0.186 0.182
    iT a l and c a 5
    Yuoveta
    2.77
    2.77 0.05 0.05
    0/1
    0.1 0.02
    at
    0.02 0.05
    0.05 E, start of the reaction from 0.05 0.05 0.05 0.05 E / j calculation from AE reading E, start of reaction from 0.050.05 0.05 reading E, calculation from Е2-Е ЛЕ 1,1130,728 1,100
    Components Incubation 1 min at, reading defenol oxidase, 0.2% 0.05 Incubation 17 min at 25 seconds reading LE0.890 claims 1. Method for the determination of substrate or enzymatic activity in biological material by performing a redox reaction, characterized by that, in order to improve the accuracy of the process, asbestos in the amount of 100 Eff / mp of the initial mixture are added to the reaction mixture, and the reaction is taken into account when a colored product is formed. 2. A method according to claim 1, characterized in that, to obtain a colored product, ascorbate oxidase is administered simultaneously with the H O of the enzyme.
    Continued tabl ..
    Cuvette E, start of reaction with 0.05 0.05 E calculation from E „-E. DE 0.485 G, 896 3. The method according to claim 1, characterized in that, to obtain a colored product, ascorbate oxidase is administered simultaneously with the tetrazole salt. 4. The method according to claim 1, characterized by and with t-em that, to obtain a colored product, ascorbate oxidase is introduced simultaneously with phenol. 5, a method according to claim 1, characterized in that Zucchini ascorbate oxidase (Cucurbuta rero medunos a) is used. Sources of information taken into account in the examination 1. Biochemical Copper Proceedings. "Tarriman, N.V. 1965, p. 305-337.
    权利要求:
    Claims (5)
    [1]
    Claim
    1. The method of determining the substrate or enzymatic activity in biological material by conducting a redox reaction, characterized in that, in order to improve the accuracy of the method, ascorbate oxidase is added to the reaction mixture in an amount
    100 U "/ ml of the initial mixture, and the reaction is carried out according to the formation of a colored product.
    [2]
    2. The method according to claim 1, characterized in that, to obtain a colored product, ascorbate oxidase is administered simultaneously with H ^ O ^ forming enzyme.
    [3]
    3. The method according to claim 1, characterized in that in order to obtain a colored product, ascorbate oxidase is administered simultaneously with the tetrazolium salt.
    [4]
    4. The method according to claim 1, characterized in that in order to obtain a colored product ascorbate oxidase is introduced simultaneously with phenol.
    [5]
    5. The method according to claim 1, characterized in that they use ascorbate oxidase from Zucchini (Cucurbuta pepo medu J1oia).
    30 Sources of information,
    Taken into account during the examination
    1. Biochemical Copper Proceedings.
    Harriman, N.V. 1965, c. 305-337.
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    同族专利:
    公开号 | 公开日
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    AU500988B2|1979-06-07|
    IT1075527B|1985-04-22|
    AR212763A1|1978-09-29|
    DK202677A|1977-12-10|
    IL52047A|1981-09-13|
    IE45546L|1977-12-09|
    PL114343B1|1981-01-31|
    NL169503C|1982-07-16|
    DD130178A5|1978-03-08|
    GB1519134A|1978-07-26|
    DE2625834C3|1989-11-23|
    ES458544A1|1978-04-16|
    NL169503B|1982-02-16|
    CH633887A5|1982-12-31|
    NL7704591A|1977-12-13|
    FR2354561A1|1978-01-06|
    NO771599L|1977-12-12|
    NO148340B|1983-06-13|
    FI771356A|1977-12-10|
    FI60719B|1981-11-30|
    DE2625834A1|1977-12-15|
    ZA772716B|1978-05-30|
    IL52047D0|1977-07-31|
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    CS235068B2|1985-04-16|
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    法律状态:
    优先权:
    申请号 | 申请日 | 专利标题
    DE2625834A|DE2625834C3|1976-06-09|1976-06-09|
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