Khachidze D G, Monaselidze D R
Institute of Physics, Academy of Sciences of Georgia, Tbilisi, Georgia.
Biofizika. 2000 Mar-Apr;45(2):320-4.
It was established that albumin of donor blood serum denatures in two temperature ranges. It is shown that the first stage of denaturation with Td = 61.5 degrees C is dominant and corresponds to melting of regions not bound to fatty acids. The second stage with Td = 80 degrees C corresponds to melting of regions bound to fatty acids. Serum denaturation heat is equal to 20.2 J/g dry protein. A change in denaturation heat capacity is 0.21 J/(g.K). Analysis of thermal parameters of deconvolution peaks showed that albumin of donor blood serum is in a fatless state and its multiple binding centers are essentially free as compared with freshly isolated albumin and may play an important role in binding of ligands in vivo. The thermal parameters of denaturation of some important human blood serum proteins including gamma-globulins, transferrin ceruloplasmin and protease inhibitors were also determined.
已确定供体血清白蛋白在两个温度范围内变性。结果表明，变性的第一阶段（变性温度Td = 61.5℃）占主导地位，对应于未与脂肪酸结合区域的熔化。第二阶段（Td = 80℃）对应于与脂肪酸结合区域的熔化。血清变性热等于20.2 J/g干蛋白。变性热容量变化为0.21 J/(g·K)。对去卷积峰热参数的分析表明，供体血清白蛋白处于无脂肪状态，与新鲜分离的白蛋白相比，其多个结合中心基本是自由的，可能在体内配体结合中起重要作用。还测定了一些重要的人血清蛋白（包括γ-球蛋白、转铁蛋白、铜蓝蛋白和蛋白酶抑制剂）的变性热参数。
