Hilz H, Wiegers U, Adamietz P
Eur J Biochem. 1975 Aug 1;56(1):103-8. doi: 10.1111/j.1432-1033.1975.tb02211.x.
Hydrolysis of serum albumin by proteinase K was strongly (greater than 7-fold) stimulated by urea and dodecylsulfate in a dose-dependent manner. With an oligopeptide as substrate, however, proteinase K was inactivated by dodecylsulfate. This indicates that the apparent activation of proteinase K by urea and dodecylsulfate is caused primarily by denaturation of the protein substrates. Although dodecylsulfate inhibited ribonuclease activity in the test-tube completely, it could not prevent RNA degradation during isolation of polysomal RNA, to which ribonuclease had been added, because of the reversible nature of the dodecylsulfate inhibition. Complete protection of RNA, however, was achieved by a combination of dodecylsulfate and proteinase K. The combined action of the detergent and proteinase K was also effective in degrading "masked" proteins in a poly(adenosine diphosphoribose) preparation which could not be attacked by the proteinase alone.
蛋白酶K对血清白蛋白的水解作用受到尿素和十二烷基硫酸盐的强烈刺激（超过7倍），且呈剂量依赖性。然而，以寡肽为底物时，蛋白酶K会被十二烷基硫酸盐灭活。这表明尿素和十二烷基硫酸盐对蛋白酶K的明显激活主要是由蛋白质底物的变性引起的。尽管十二烷基硫酸盐在试管中能完全抑制核糖核酸酶的活性，但由于其抑制作用的可逆性，在添加了核糖核酸酶的多聚核糖体RNA分离过程中，它无法阻止RNA的降解。然而，通过十二烷基硫酸盐和蛋白酶K的联合使用可实现对RNA的完全保护。去污剂和蛋白酶K的联合作用在降解聚（腺苷二磷酸核糖）制剂中“隐蔽”的蛋白质方面也很有效，而这些蛋白质单独用蛋白酶无法攻击。
