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本文用差示扫描量热计,在274—345K温度范围内,研究了Ⅰ型人胎盘胶原在各种水介质中的热变性过程,测得这些过程的热力学参数。在pH3.7无盐水溶液中,该胶原的平均变性温度T_d为47.1℃,变性焓△H_d为8.43kJ/mol残基。得到各种胶原的△H_d-T_d的线性函数关系,指明人胎盘胶原结构稳定化的各种因素。用热力学事实判定水-羰基模型是更可取的。通过van’t Hoff焓的计算估计出入胎盘胶原分子中有5个合作块,每个合作块包含600个残基,是多区域蛋白质。
In this paper, with the differential scanning calorimeter, in the temperature range of 274-345K, the thermal denaturation process of Type I human placental collagen in various aqueous media was studied, and the thermodynamic parameters of these processes were measured. The average denaturation temperature T_d of this collagen was 47.1 ℃ and the enthalpy △ H_d of 8.43kJ / mol residues in pH3.7 saline-free solution. The linear function of △ H_d-T_d of various collagen was obtained, indicating various factors of human placental collagen structure stabilization. Judging the water-carbonyl model with thermodynamic facts is preferable. The van’t Hoff enthalpy calculation estimates that there are five cooperating blocks in the placental collagen molecule, each of which contains 600 residues and is a multi-domain protein.