在含有苯酚的溶剂混合物中牛血清白蛋白和α-胰凝乳蛋白酶原A的性质
The properties of bovine serum albumin and chymotrypsinogen A in solvent mixtures containing phenol.
作者信息
Pusztai A
出版信息
Biochem J. 1966 Nov;101(2):265-73. doi: 10.1042/bj1010265.
Abstract
- The optical rotation and reduced viscosity of bovine serum albumin and chymotrypsinogen A in solvents containing phenol, acetic acid and water were studied. 2. The changes brought about in the properties of the proteins by varying the composition of the solvent or by heat treatment in these solvents were established to be reversible. 3. A method for returning the proteins to aqueous media, based on these observations, was worked out. 4. The recovered proteins were shown to be very similar to, if not identical with, the native proteins on the basis of measurements of optical rotation, viscosity, sedimentation, ultraviolet spectroscopy, immunochemical behaviour (serum albumin) and proteolytic activity (chymotrypsinogen A, after activation with trypsin). 5. The importance of the findings for partitioning of polyelectrolytes in the phenol-aqueous buffer systems is discussed.
摘要
- 研究了牛血清白蛋白和α-胰凝乳蛋白酶原A在含有苯酚、乙酸和水的溶剂中的旋光性和比浓粘度。2. 通过改变溶剂组成或在这些溶剂中进行热处理而引起的蛋白质性质变化被确定为是可逆的。3. 基于这些观察结果，制定了一种将蛋白质重新转移到水性介质中的方法。4. 根据旋光性、粘度、沉降、紫外光谱、免疫化学行为（血清白蛋白）和蛋白水解活性（用胰蛋白酶激活后的α-胰凝乳蛋白酶原A）的测量结果，回收的蛋白质被证明即使与天然蛋白质不完全相同，也非常相似。5. 讨论了这些发现对于聚电解质在苯酚-水性缓冲体系中分配的重要性。
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