dc.creatorRover, L
dc.creatorFernandes, JCB
dc.creatorNeto, GD
dc.creatorKubota, LT
dc.creatorKatekawa, E
dc.creatorSerrano, SHP
dc.date1998
dc.date42156
dc.date2014-12-02T16:24:42Z
dc.date2015-11-26T17:18:39Z
dc.date2014-12-02T16:24:42Z
dc.date2015-11-26T17:18:39Z
dc.date.accessioned2018-03-29T00:06:20Z
dc.date.available2018-03-29T00:06:20Z
dc.identifierAnalytical Biochemistry. Academic Press Inc, v. 260, n. 1, n. 50, n. 55, 1998.
dc.identifier0003-2697
dc.identifierWOS:000074272500007
dc.identifier10.1006/abio.1998.2656
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/75294
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/75294
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/75294
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1282710
dc.descriptionThe chemical stability of nicotinamide adenine dinucleotide coenzyme (NADH/NAD(+)) and its derivatives (NADPH/NADP(+)) was investigated using changes in the UV-visible absorption spectra of these compounds. The spectra of cofactor (reduced form) were monitored at 340 nm wavelength in different buffers, showing a faster degradation in phosphate buffer. This was assigned to the adduct formation between phosphate and NADH (pyridine ring). The three-factor-two-level factorial design study evaluated the contributions: buffers (phosphate and Pipes 0.1 M), pH's (6.8 and 7.8), and temperature (25 and 30 degrees C). The freshly prepared aqueous solutions of coenzyme were analyzed after 40 min under the different conditions (eight assays in triplicate) of the experiment. The main observed effects of the NADH oxidation were, in increasing order, pH, temperature, and buffer without appreciable interactive effects. Therefore, it was verified that the better conditions for cofactor use were alkaline media employing Pipes buffer or its derivatives and low temperatures. (C) 1998 Academic Press.
dc.description260
dc.description1
dc.description50
dc.description55
dc.languageen
dc.publisherAcademic Press Inc
dc.publisherSan Diego
dc.publisherEUA
dc.relationAnalytical Biochemistry
dc.relationAnal. Biochem.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectNADH
dc.subjectchemical stability
dc.subjectfactorial design
dc.subjectFlow-injection Analysis
dc.subjectElectrocatalytic Oxidation
dc.subjectEnzyme Electrode
dc.subjectMeldolas-blue
dc.subjectDehydrogenase
dc.subjectSalicylate
dc.subjectBiosensor
dc.subjectRegeneration
dc.subjectInhibition
dc.subjectLactate
dc.titleStudy of NADH stability using ultraviolet-visible spectrophotometric analysis and factorial design
dc.typeArtículos de revistas


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