Abstract
ABSTRACTSpectrophotometry is employed to study the effect cetyltrimethylammonium bromide (CTAB) and bis(cetyldimethylammonium)butane dibromide (C16C4C16Br2) on the activity of xanthine oxidase (XO), a key enzyme in purine metabolism, at pH 7.4 and 25°C. The spectrophotometric results revealed that the Gemini surfactant interact strongly with the XO than its conventional single chain counterpart and unfold it to a greater extent as compared to CTAB. The effectiveness of the Gemini in interacting/unfolding the XO are justified owing to peculiar structural features of C16C4C16Br2 owing to the presence of two charged headgroups and two hydrophobic tails and hence enhanced competence for electrostatic and hydrophobic interactions.
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