Prieels J P, Schlusselberg J
Biochim Biophys Acta. 1977 Mar 28;491(1):76-81. doi: 10.1016/0005-2795(77)90042-3.
alpha-Lactalbumin from human milk shows an heterogeneous behaviour when subjected to ion exchange chromatography with DEAE-Sephadex. Two components have been separated, showing identical patterns in the following studies: amino acid compositions, fluorescence and circular dichroism spectra, transition temperature of denaturation, antigenicity, lactose synthase specifying activity and hydrodynamic properties. After rechromatography of either peak, these two components appeared to be in equilibrium. This equilibrium varies with the temperature and the pH of chromatography. Moreover, an increase of n-alcohol concentration in the eluting buffer also induces an increase of the second protein peak eluting at higher ionic strength. These two peaks seem to be the result of some conformational change induced upon the binding of the protein to the solid anionic matrix.
人乳中的α-乳白蛋白在用DEAE-葡聚糖进行离子交换色谱分析时表现出异质性。已分离出两种成分，在以下研究中显示出相同的模式：氨基酸组成、荧光和圆二色光谱、变性转变温度、抗原性、乳糖合酶特异性活性和流体动力学性质。对任一峰进行再色谱分析后，这两种成分似乎处于平衡状态。这种平衡随色谱温度和pH值而变化。此外，洗脱缓冲液中正醇浓度的增加也会导致在较高离子强度下洗脱的第二个蛋白峰增加。这两个峰似乎是蛋白质与固体阴离子基质结合时诱导的某种构象变化的结果。
