Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/928
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dc.contributor.authorSun, Wei-
dc.contributor.authorZhao, Na-
dc.contributor.authorJiao, Kui-
dc.date.accessioned2008-04-10T10:24:59Z-
dc.date.available2008-04-10T10:24:59Z-
dc.date.issued2007-02-
dc.identifier.issn0376-4710-
dc.identifier.urihttp://hdl.handle.net/123456789/928-
dc.description280-283en_US
dc.description.abstractA new electrochemical method is proposed for the determination of trace amounts of proteins using arsenazo I as a voltammetric probe. At pH 1.5 Britton-Robinson buffer solution, arsenazo I has a sensitive second order derivative linear sweep voltammetric reductive peak at -0.23 V (vs. SCE). The addition of human serum albumin into the dye solution decreases the reductive peak current without change of peak potential, indicating that HSA can interact with arsenazo I to form a supramolecular complex. The decrease of peak current is proportional to the concentration of HSA, which can be further used for the HSA determination. The optimal conditions of the binding reaction and the electrochemical detection have been investigated. The binding constant (βs) and the binding number (m) of human serum albumin with arsenazo I have been calculated as βs= 3.9×10¹⁷ and m= 4. No changes are observed in the electrochemical parameters of the reaction system indicating that an electro-inactive complex is formed in the mixed solutions.en_US
dc.language.isoen_USen_US
dc.publisherCSIRen_US
dc.relation.ispartofseriesInt. Cl.⁸ G01N27/00en_US
dc.sourceIJCA Vol.46A(2) [February 2007]en_US
dc.titleElectrochemical determination of proteins using arsenazo I as voltammetric probeen_US
dc.typeArticleen_US
Appears in Collections:IJC-A Vol.46A(02) [February 2007]

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