Dzhafarov E S
Mol Biol (Mosk). 1991 Sep-Oct;25(5):1412-7.
Accessible surfaces of the HSA molecule in N-, F- and B-forms were studied in the present work by tritium labelling method which allowed to obtain detailed information on N-F- and N-B-transitions. In was shown that the F-form in comparison top the N-form is characterized by more high accessibility of Ser, Ala, Ile, Tyr, Phe, His, Arg, Pro, Val and Phe residues and in the B-form Tyr, Ser, Arg, Gly, Ile, Phe and Pro residues turn to be highly accessible. Full accessible surfaces of protein molecule at N-F- and N-B-transitions increase respectively from 39,000 to 70,400 A2 and from 39,000 to 47,000 A2. Basing on the prevailing increase of hydrophobic residues accessibility it is supposed that the molecule expansion testifies the separation of the subunits forming the molecule.
在本研究中，采用氚标记法对人血清白蛋白（HSA）分子N型、F型和B型的可及表面进行了研究，该方法能够获取有关N - F和N - B转变的详细信息。结果表明，与N型相比，F型的特点是Ser、Ala、Ile、Tyr、Phe、His、Arg、Pro、Val和Phe残基的可及性更高，而在B型中，Tyr、Ser、Arg、Gly、Ile、Phe和Pro残基的可及性很高。在N - F和N - B转变过程中，蛋白质分子的完全可及表面分别从39,000 Ų增加到70,400 Ų和从39,000 Ų增加到47,000 Ų。基于疏水残基可及性的普遍增加，推测分子的扩张证明了构成分子的亚基的分离。
