Sjödin T, Hansson R, Sjöholm I
Biochim Biophys Acta. 1977 Sep 27;494(1):61-75. doi: 10.1016/0005-2795(77)90135-0.
Extensive digestion of human serum albumin with trypsin at pH 8.8 yields essentially one main fragment which is resistant to further tryptic degradation. The fragment has been characterized by amino acid analysis, N- and C-terminal analyses, cyanogen bromide digestion, electrophoresis, ultracentrifugation and gelfiltration, and circular dichroism measurements. The results indicate that the main fragment consists of the amino acids 182-585. Repeated digestion did not degrade the isolated fragment further. The fragment mainly retains the secondary and tertiary structure of intact human serum albumin as well as its capacity to bind bilirubin and diazepam. The localization of the binding sites for these substances is discussed.
在pH 8.8条件下用胰蛋白酶充分消化人血清白蛋白，基本上会产生一个主要片段，该片段对进一步的胰蛋白酶降解具有抗性。已通过氨基酸分析、N端和C端分析、溴化氰消化、电泳、超速离心和凝胶过滤以及圆二色性测量对该片段进行了表征。结果表明，主要片段由氨基酸182 - 585组成。重复消化并未使分离出的片段进一步降解。该片段主要保留了完整人血清白蛋白的二级和三级结构以及其结合胆红素和地西泮的能力。文中讨论了这些物质结合位点的定位。
