Study on interaction between p-hydroquinone and cattle serum protein
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Abstract
Objective To explore the interaction between p-hydroquinone and serum protein.Methods The cyclic voltammetry(CV)of p-hydroquinone and conjoint p-hydroquinone with serum protein at L-cysteine bodified golden electrode in 0105 mol/L Na2HPO4-0.05 mol/L NaH2PO4-0.110 mol/L NaCl buffer solution(pH=7.30)was studied in this paper.Results The peak of conjointhydroquinone with serum protein shifted to positive,the current of conjoint p-benzoquionone with serum protein decreased,and peak of conjoint p-benzoquionone with serum protein shifted to negative.According to the saturation of respective conjointhydroquinone and p-benoquionone with serum protein,the conjoint rate of hydroquinone and p-benzoquionone with serum protein was 48:1 and 16:1 respectively.Conclusion The interaction between p-hydroquinone and serum protein ascribes to hydrogen bonding,however,this force between serum protein and pbenzoquionone is more than that between p-hydroquinone and serum protein.
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