Corbett R J, Roche R S
Int J Pept Protein Res. 1986 Dec;28(6):549-59. doi: 10.1111/j.1399-3011.1986.tb03292.x.
High molecular weight autolysis products from thermolysin have been isolated and identified. The primary fragments correspond to residues 1 to 187-204 (21kD) and residues 187-204 to 316 (12kD), respectively. The fragments are both capable of independent refolding upon removal of denaturant. On the basis of these results, we suggest that the first step in the unfolding pathway of thermolysin involves unfolding of an interdomain region and domain separation. Bound calcium ions at sites 1, 2 and 4 play a major role in protecting the protein against both autolysis and unfolding, probably by stabilizing the interdomain region and enhancing domain-domain interactions.
已分离并鉴定了嗜热菌蛋白酶的高分子量自溶产物。主要片段分别对应于残基1至187 - 204（21kD）和残基187 - 204至316（12kD）。这些片段在去除变性剂后均能独立重折叠。基于这些结果，我们认为嗜热菌蛋白酶展开途径的第一步涉及结构域间区域的展开和结构域分离。位点1、2和4处结合的钙离子在保护蛋白质免于自溶和展开方面起主要作用，可能是通过稳定结构域间区域并增强结构域 - 结构域相互作用来实现的。
