Zizkovský V, Strop P, Lukesová S, Korcáková J, Dvorák P
Oncodev Biol Med. 1981;2(5):323-30.
Human alpha-fetoprotein (AFP) and serum albumin (HSA) were studied by hydrophobic interaction chromatography. A close resemblance was observed both in the native state and after various perturbations (pH, salt and alcohol) indicating a significant similarity in their molecular structures. Both proteins displayed similar hydrophobic properties which apparently were different from those of other globular proteins. In agreement with the domain structure proposed by Brown (1976), our results indicated that surface nonpolar side chains of both the native HSA and AFP produced large hydrophobic areas located solely in crevices.
采用疏水相互作用色谱法对人甲胎蛋白（AFP）和血清白蛋白（HSA）进行了研究。在天然状态以及经过各种扰动（pH值、盐和醇）后，观察到二者极为相似，表明它们的分子结构具有显著的相似性。两种蛋白质均表现出相似的疏水特性，这显然不同于其他球状蛋白质。与Brown（1976年）提出的结构域结构一致，我们的结果表明，天然HSA和AFP的表面非极性侧链均产生了仅位于裂隙中的大疏水区域。
