Cross G A
J Cell Biochem. 1984;24(1):79-90. doi: 10.1002/jcb.240240107.
Conditions affecting the solubilization of variant surface glycoprotein (VSG) from Trypanosoma brucei have been investigated. The results obtained form the basis for a convenient and efficient method for VSG purification. VSG release from the cell surface was temperature-dependent, following osmotic lysis at 0 degree C, and was inhibited by low concentrations of Zn2+ but not by tosyl-lysine chloromethyl-ketone (TLCK), phenylmethylsulfonylfluoride (PMSF), or iodoacetamide. These and other results eliminated the possibility that release was due to proteolytic cleavage of the C-terminal hydrophobic tail present on newly synthesized VSG. Bolton and Hunter reagent reacted with several components on living cells.
对影响布氏锥虫可变表面糖蛋白（VSG）溶解的条件进行了研究。所获得的结果为一种简便高效的VSG纯化方法奠定了基础。VSG从细胞表面的释放取决于温度，在0℃进行渗透裂解后发生，并且受到低浓度Zn2 +的抑制，但不受甲苯磺酰赖氨酸氯甲基酮（TLCK）、苯甲基磺酰氟（PMSF）或碘乙酰胺的抑制。这些结果以及其他结果排除了释放是由于新合成的VSG上存在的C末端疏水尾部发生蛋白水解切割所致的可能性。博尔顿-亨特试剂与活细胞上的几种成分发生反应。
