A Microcalorimetry and Spectroscopy Study on the Interaction of BSA with 2,2′-Bipyridine Octylglycinato Palladium(II) Nitrate
A Microcalorimetry and Spectroscopy Study on the Interaction of BSA with 2,2′-Bipyridine Octylglycinato Palladium（II） Nitrate作者机构：Institute of Biochemistry and Biophysics Department of Chemistry Institute of Biochemistry and Biophysics University of Tehran Tehran 14176-14411 Iran Department of Chemistry University of Sistan & Bluchestan Zahedan 98167-45345 Iran University of Sistan & Bluchestan Zahedan 98167-45345 Iran University of Tehran Tehran 14176-14411 Iran
出 版 物：《Acta Biochimica et Biophysica Sinica》 (生物化学与生物物理学报(英文版))
年 卷 期：2003年第35卷第10期
页 面：886-890页
核心收录：
学科分类：0710[理学-生物学] 0831[工学-生物医学工程（可授工学、理学、医学学位）] 071010[理学-生物化学与分子生物学] 081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 0703[理学-化学]
主 题：serum albumin palladium complex isothermal titration microcalorimetry spectrophotometry
摘 要：The interaction of bovine serum albumin (BSA) with a new palladium(II) complex [Pd(bpy)(Oct-Gly)]NO 3 (bpy, 2,2′-bipyridine; Oct-Gly, octyl-glycine) was studied by isothermal titration UV-visible spectrophotometry and microcalorimetry in 30 mmol/L Tris buffer, pH 7.0. There is a set of 18 binding sites for this complex on BSA at 300 and 310 K with positive cooperativity in the binding process. The Hill coefficients at 300 and 310 K are 2.2 and 2.4, respectively. The binding of this palladium complex on BSA is endothermic with mean association binding constant of 21.0 and 16.4 (mmol/L) -1 at 300 and 310 K, respectively. The complex can denature the protein as surfactants. The stability of BSA in the interaction study with the complex is 84 and 58 kJ/mol at 300 and 310 K, respectively. Also, the enthalpy of BSA denaturation due to the interaction with the complex is 842 kJ/mol.
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