Volynskaia A V, Skripkin A Iu, Dzhafarov E S, Rumiantsev Iu M, Shishkov A V
Mol Biol (Mosk). 1985 Sep-Oct;19(5):1294-300.
Amino acids composing an accessible surface of lysozyme and human serum albumin (HSA) globules were determined by the total tritium labelling method. A good correlation between our data on the distribution of the tritium label for the lysozyme molecule and X-ray data on the tertiary structure for this macromolecule was received. Lysozyme was used as a standard for determining the accessible surface of the globule albumin. It was shown that the accessible surface of the albumin globule is substantially more hydrophobic (average accessible surface area of hydrophobic amino acids is 130 A2 in HSA and 20 A2 in lysozyme) than in lysozyme. The HSA molecule is characterized by high values of: the accessible surface area, the ratio of extended area to the folded one, and the surface roughness index. These data indicate that the HSA molecule is less compactly packed than lysozyme.
采用全氚标记法测定了构成溶菌酶和人血清白蛋白（HSA）球状体可及表面的氨基酸。我们获得了溶菌酶分子的氚标记分布数据与该大分子三级结构的X射线数据之间的良好相关性。溶菌酶被用作确定球状白蛋白可及表面的标准。结果表明，白蛋白球状体的可及表面比溶菌酶的可及表面疏水性更强（HSA中疏水性氨基酸的平均可及表面积为130 Ų，溶菌酶中为20 Ų）。HSA分子的特征在于具有较高的值：可及表面积、伸展面积与折叠面积之比以及表面粗糙度指数。这些数据表明，HSA分子的堆积不如溶菌酶紧密。
