论文部分内容阅读
在310.15 K，pH=7.0的生理条件下，利用微量热法研究了牛血清白蛋白与Cu2+，Ca2+相互作用，得到牛血清白蛋白与Cu2+的结合数为1；摩尔结合焓为-22.83 kJ·mol-1，摩尔结合自由能和熵分别为-66.024 kJ·mol-1和654.66 J·mol-1，而牛血清白蛋白与Ca2+则表现出较弱的相互作用.
The interaction between bovine serum albumin and Cu2 + and Ca2 + was studied by microcalorimetry under the condition of 310.15 K and pH = 7.0. The binding number of bovine serum albumin and Cu2 + was 1 and the molar enthalpy of binding was -22.83 kJ · mol-1, the molar free energy and entropy were -66.024 kJ · mol-1 and 654.66 J · mol-1, respectively, whereas bovine serum albumin and Ca2 + showed weaker interaction.