Hydroquinone Interaction with Bovine Serum Albumin.docVIP

 PAGE \* MERGEFORMAT 13 Hydroquinone Interaction with Bovine Serum Albumin 【Abstract】 Objective To explore the interaction of hydroquinone with serum albumin. Method 0  05mol / L Na2HPO4-0  05mol / L NaH2PO4-0  10mol / L NaCl buffer solution (pH = 7  30), observation of hydroquinone and bovine serum albumin with the combination of hydroquinone In the L  cysteine-modified gold electrodes on the electrochemical behavior. The results of bovine serum albumin combined with hydroquinone can hydroquinone oxidation peak potentials are shifted to restore the peak potential shifted negatively, and so benzoquinone reduction peak current decreases, based on the hydroquinone , benzoquinone, and serum albumin saturation, calculated hydroquinone, benzoquinone, and serum albumin ratio were 48:1 and 16:1. Conclusion bovine serum albumin and hydroquinone combined with a strong hydrogen bonding combination of benzoquinone with serum albumin binding greater. Keywords: hydroquinone Proteins are the basic constituents of organisms, such as enzymes, antibodies, transport proteins such as playing an important biological function of the body. Human serum albumin present in blood, the molecular weight of 66241 and isoelectric point of 4  7 〔1〕, primarily the maintenance of plasma colloid osmotic pressure, with many of its other function is slightly soluble in water, soluble in the material combination of the water complex. Phenolic compounds on DNA damage in varying degrees 〔〕 2-5, hydroquinone oxidation in the environment easily benzoquinone, hydroquinone and benzoquinone can be the formation of DNA adducts bases 〔 6-8〕 great harm on the human body. Hydroquinone and benzoquinone transit through the human serum albumin into the人体各器官. Therefore, the study of serum albumin with the hydroquinone and benzoquinone interaction of great significance. In this paper, cyclic voltammetry of hydroquinone in the L  cysteine-modified gold electrodes on the electr