Ledward D A, Finch A, Rickert W S
Biochim Biophys Acta. 1975 Feb 27;379(2):426-30. doi: 10.1016/0005-2795(75)90149-x.
The thermal denaturation of Mucor meihei protease was studied as a function of pH by differential scanning calorimetry. In both citric acid-Na2HPO4 and in acetic acid-sodium acetate buffers, maximum thermal stability was at pH 4.0-4.2. However, the maximum enthalpy changes associated with the denaturation process were buffer-dependent and occurred between pH values of 4.7 and 5.7.
通过差示扫描量热法研究了米黑根毛霉蛋白酶的热变性与pH的关系。在柠檬酸-Na2HPO4缓冲液和乙酸-乙酸钠缓冲液中，最大热稳定性均出现在pH 4.0 - 4.2。然而，与变性过程相关的最大焓变取决于缓冲液，且发生在pH值4.7至5.7之间。
