The Binding of Sodium Nitroprusside with Albumin Using Square Wave Voltammetry | Zendy

Mohammed M. A. Abdullah Al-Imam | Zendy; S.T. Sulaiman | Zendy

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The Binding of Sodium Nitroprusside with Albumin Using Square Wave Voltammetry

Author(s) -

Mohammed M. A. Abdullah Al-Imam,

S.T. Sulaiman

Publication year - 2012

Publication title -

mağallaẗ ʻulūm al-rāfidayn

Language(s) - English

Resource type - Journals

eISSN - 2664-2786

pISSN - 1608-9391

DOI - 10.33899/rjs.2012.44368

Subject(s) - sodium nitroprusside , chemistry , voltammetry , aqueous solution , analytical chemistry (journal) , sodium , cyclic voltammetry , binding constant , inorganic chemistry , chromatography , electrode , electrochemistry , binding site , organic chemistry , biochemistry , nitric oxide

The voltammetric behavior of pure Sodium Nitroprusside was studied in a direct method in aqueous phosphate solution at (pH=7.0) by square wave voltammetry Sodium Nitroprusside gives a well defined square wave voltammetric peak at (-0.592) volt against the reference electrode (Ag/AgCl/SatKCl). The calibration curve is linear within the range of concentration [(0.398 ×10 -6 ) – (8.424×10 -6 )] molar with a correlation coefficient of (0.9991). The binding of Sodium Nitroprusside with Albumin has been studied, the binding constants (K) were calculated at different temperatures. Vant's hoff equation applied to calculate the thermodynamic variables (∆G,∆S,∆H), and the results indicate that the binding of SNP with albumin is of the type (ion-ion).

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