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Method for Highly Sensitive Determination of NADH Using NADH Kinase

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Method for Highly Sensitive Determination of NADH Using NADH Kinase Europaisches Patentamt European Patent Office © Publication number: 0 496 412 A2 Office europeen des brevets EUROPEAN PATENT APPLICATION © Application number: 92101139.1 © int.ci.5:C12Q 1/48, //C12Q1/32 @ Date of filing: 24.01.92 ® Priority: 25.01.91 JP 7999/91 © Applicant: NODA INSTITUTE FOR SCIENTIFIC RESEARCH @ Date of publication of application: 399 Noda 29.07.92 Bulletin 92/31 Noda-shi Chiba-ken(JP) Applicant: INTERNATIONAL REAGENTS © Designated Contracting States: CORPORATION DE FR GB 1-30, Hamabe-dori 2-chome Chuo-ku Kobe-shi Hyogo-ken(JP) @ Inventor: Ohno, Tsuyoshi 379-4-302, Nemoto Matsudo-shi(JP) Inventor: Suzuki, Masaru 572-25, Nakanokuki Nagareyama-shi(JP) Inventor: Horiuchi, Tatsuo 126-55-409, Higashihatsuishi-3-chome Nagareyama-shi(JP) Inventor: Shirahase, Yasushi 8-3-532-305, Gakuennishimachi-5-chome Nishi-ku, Kobe-shi(JP) Inventor: Kishi, Koji 1- 13-202, Kamitakamaru-2-chome Tarumi-ku, Kobe-shi(JP) Inventor: Watazu, Yoshifumi 2- 804, Saenbacho-3-chome Akashi-shi(JP) © Representative: Hansen, Bernd, Dr. Dipl.-Chem. et al Hoffmann, Eitle & Partner Patent- und Rechtsanwalte Arabellastrasse 4 Postfach CM 81 04 20 < W-8000 Munchen 81 (DE) CM © Method for highly sensitive determination of NADH using NADH kinase. CO Oi © The present invention relates to a method for determining a slight amount of NADH or XTP which is present in a solution, with high sensitivity by the use of an NADH kinase specific for NADH by utilizing a cycling reaction, and this method permits highly sensitive determination of NADH without any influence of NAD and hence is useful for diagnoses of diseases and the like. Rank Xerox (UK) Business Services EP 0 496 412 A2 BACKGROUND OF THE INVENTION The present invention permits accurate diagnoses mainly of diseases and the like by highly sensitive determination of a substance capable of serving as a marker of pathosis, by the use of an NADH kinase 5 highly specific for NADH, and can be utilized in the fields of clinical diagnoses, therapeutics, etc. DESCRIPTION OF THE PRIOR ART Now, there is widely employed a diagnostic method in which the amount of a substance capable of io serving as a marker of pathosis is determined using an enzymatic reaction. However, there exist trace markers which are difficult to measure by conventional methods, and the amount of a test fluid is limited to a slight amount in some cases, for example, medical examinations of newborn babies. Highly sensitive analytical methods capable of solving such problems are desirable. One of such methods is a sensitizing analytical method using a cycling reaction. As the cycling 75 reaction, there are known /3-NAD ** /3-NADH cycling reaction, /3-NADP ** /3-NADPH cycling reaction, etc. ["Seikagaku Jikken Koza (Biochemical Experiments)", Vol. 5, p. 121-131]. For example, as disclosed in Japanese Patent Unexamined Publication No. 59-213400, /3-NAD can be determined with high sensitivity by phosphorylating only /3-NAD in a solution containing /3-NADH and /3-NAD , into /3-NADP by the use of a kinase specific for /3-NAD , and subjecting the /3-NADP to the cycling reaction. 20 However, when a slight amount of NADH is present in a mixture comprising NAD (hereinafter referring to /3-NAD+, thio-NAD+ or a-NAD+) and NADH (/3-NADH, thio-NADH or /3-NADH), it cannot be determined by the above method disclosed in Japanese Patent Unexamined Publication No. 59-213400. Therefore, there have heretofore been employed a flow injection assay using HPLC and a method comprising boiling (Japanese Patent Unexamined Publication No. 58-129994), but there methods are disadvantageous in that 25 they require an expensive apparatus, a troublesome procedure and a long time. There are also a highly sensitive method comprising allowing /3-NADH to cause luminescence by the use of luciferase and a method comprising allowing /3-NADH to cause chemiluminescence, but these methods require a special and expensive detector and involve the problem of the stability of reagents. 30 SUMMARY OF THE INVENTION In consideration of such conditions, the present inventors earnestly investigated a method for determin- ing a slight amount of NADH with high sensitivity in the case where excess NAD is present. Consequently, it was found that this purpose can be achieved by the use of a kinase which acts specifically on NADH. As 35 a result of further investigation, the present inventors found that also in a mixture comprising NAD and a slight amount of NADH, NADH can be determined with high sensitivity by phosphorylating only NADH into NADPH and subjecting the NADPH to the cycling reaction, and that highly sensitive determination of a slight amount of XTP can also be made possible, whereby the present invention was accomplished. The present invention provides a method for highly sensitive determination of NADH which comprises 40 allowing an NADH kinase highly specific for NADH to act on a solution containing NAD and NADH, in the presence of divalent metal ions and XTP [wherein X is A (adenosine), U (uridine), G (guanosine), C (cytidine), I (inosine), dT (thymidine), dA (deoxyadenosine), dU (deoxyuridine), dG (deoxyguanosine), dC (deoxycytidine), or dl (deoxyinosine)], to produce XDP (wherein X is as defined above) and NADPH; subjecting the NADPH to the cycling reaction by using a catalytic reaction capable of oxidizing NADPH into 45 NADP and a catalytic reaction capable of reducing NADP into NADPH; measuring the variable amount of a substrate consumed by the cycling reaction or a product produced by the cycling reaction; and thereby determining the amount of only NADH in the mixed solution containing NAD and NADH. The present invention further provides a method for highly sensitive determination of XTP which comprises allowing an NADH kinase highly specific for NADH to act on a solution containing XTP [wherein 50 X is A (adenosine), U (uridine), G (guanosine), C (cytidine), I (inosine), dT (thymidine), dA (deoxyadenosine), dU (deoxyuridine), dG (deoxyguanosine), dC (deoxycytidine), or dl (deoxyinosine)] in the presence of divalent metal ions and NADH to produce XDP (wherein X is as defined above) and NADPH; subjecting the NADPH to the cycling reaction by using a catalytic reaction capable of oxidizing NADPH into NADP and a catalytic reaction capable of reducing NADP into NADPH; measuring the variable amount of a 55 substrate consumed by the cycling reaction or a product produced by the cycling reaction; and thereby determining the amount of XTP. The above NAD+ includes /3-NAD+, thio-NAD+ and a-NAD+. The above NADH includes /3-NADH, thio- NADH and a-NADH. 2 EP 0 496 412 A2 The above divalent metal ion includes Mg2+, Mn2+, Ca2+, Co2+, etc. A catalyst for the oxidation includes dehydrogenases, diaphorases, NAD(P)H oxidase and electron carriers. The electron carriers include Meldola's Blue (9-dimethylamino-benzo-a-phenazoxonium chloride), 1-methoxy PMS (1-methoxy-5-methyl- phenazinium methylsulfate), PMS (methylphenazinium methylsulfate), PQQ (pyrroloquinoline quinone), etc. 5 A catalyst for the reduction includes dehydrogenases, and NADP -dependent dehydrogenases are particu- larly preferable. BRIEF DESCRIPTION OF THE DRAWINGS 10 In the accompanying drawings: Fig. 1 is a graph showing the optimum pH of the present enzyme ( • - • : phosphate buffer, O - O : Tris-HCI buffer, a - a: glycine-sodium hydroxide buffer). Fig. 2 is a graph showing a pH range for stability of the present enzyme ( • - •: phosphate buffer, O - O : Tris-HCI buffer, a - a: glycine-sodium hydroxide buffer). is Fig. 3 is a graph showing a range of temperature suitable for action of the present enzyme. Fig. 4 is a graph showing the thermal stability of the present enzyme. Fig. 5 shows a calibration curve obtained in Example 2 by plotting AOD60onm/nnin against NADH concentration. Fig. 6 shows a calibration curve obtained in Example 3 by plotting AOD60onm/nnin against sodium cholate 20 concentration. Fig. 7 shows a calibration curve obtained by the use of /3-NAD in Example 4 by plotting AOD60onm/nnin against sodium cholate concentration. Fig. 8 shows a calibration curve obtained by the use of thio-NAD in Example 4 by plotting AOD55onm/nnin against sodium cholate concentration. 25 Fig. 9 is a diagram showing the correlation between measured values obtained by the present method and those obtained by the 3a-HSD-formazan method which was determined in Example 5. Fig. 10 is a calibration curve obtained in Example 6 by plotting AOD60onm/nnin against the level of 3- hydroxybutylate dehydrogenase activity. Fig. 11 is a calibration curve obtained in Example 7 by plotting AOD55onm/nnin against glycerin 30 concentration. Fig. 12 is a calibration curve obtained in Example 8 by plotting AOD55onm/nnin against the level of alcohol dehydrogenase activity. Fig. 13 is a calibration curve obtained in Example 9 by plotting AOD60onm/nnin against ATP concentration. 35 DESCRIPTION OF THE PREFERRED EMBODIMENTS The present invention is explained below in detail. First, an outline of reactions in the highly sensitive determination of the present invention is shown below. 40 NADH 45 Divalent metal ions 50 55 3 EP 0 496 412 A2 wherein the symbols have the following meanings: Ei : an oxidation catalyst capable of catalyzing a reaction by which NADP+ and Pi may be produced from substrates NADPH and Si . E2 : a reduction catalyst capable of catalyzing a reaction by which NADPH and P2 may be 5 produced from substrates NADP and S2. 51 : an oxidized-form substrate for E1 . 52 : a reduced-form substrate for E2. Pi : a reduced-form product produced from Si by E1 . P2 : an oxidized-form product produced from S2 by E2. 70 XTP : X = A : adenosine-5'-triphosphate = U : uridine-5'-triphosphate = G : guanosine-5'-triphosphate = C : cytidine-5'-triphosphate = I : inosine-5'-triphosphate 75 = dT : thymidine-5'-triphosphate = dA : 2'-deoxyadenosine-5'-triphosphate = dU : 2'-deoxyuridine-5'-triphosphate = dG : 2'-deoxyguanosine-5'-triphosphate = dC : 2'-deoxycytidine-5'-triphosphate 20 = dl : 2'-deoxyinosine-5'-triphosphate XDP : each of the same compounds as above except that triphosphate is replaced by diphosphate.
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