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dc.contributor.authorMote, Umesh S-
dc.contributor.authorKolekar, G B-
dc.identifier.issn0975-0975(Online); 0376-4710(Print)-
dc.description.abstractThe interaction between bovine serum albumin (BSA) and atazanvir sulphate (AS) has been investigated under the physiological pH 7.4 condition using fluoresence spectroscopy. The binding constant, number of binding site, thermodynamic parameters such as ∆G, ∆H, ∆S and nature of binding forces between BSA-AS have been obtained from the steady state fluorescence quenching of BSA by AS. The static quenching is confirmed from Stern-Volmer quenching constant at different temperatures. The effect of AS on the conformation of BSA has been analyzed using synchronous and three-dimensional fluorescence spectroscopy.en_US
dc.publisherNISCAIR-CSIR, Indiaen_US
dc.rightsCC Attribution-Noncommercial-No Derivative Works 2.5 Indiaen_US
dc.sourceIJC-A Vol.55A(07) [July 2016]en_US
dc.subjectFluorescence quenchingen_US
dc.subjectThermodynamic parametersen_US
dc.subjectSynchronous fluorescenceen_US
dc.subjectBinding constanten_US
dc.titleInvestigations on interaction between atazanvir sulphate and bovine serum albumin by fluorescence spectroscopyen_US
Appears in Collections:IJC-A Vol.55A(07) [July 2016]

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