一项关于在盐酸胍中被抑制的枯草杆菌蛋白酶展开过程的研究。

A study of the unfolding of the inhibited subtilisin in guanidine hydrochloride.

作者信息

Contaxis C C, McBride-Warren P A, Epand R M

出版信息

Int J Pept Protein Res. 1975;7(2):135-42. doi: 10.1111/j.1399-3011.1975.tb02423.x.

DOI:10.1111/j.1399-3011.1975.tb02423.x

Abstract

Inhibited subtilisin (Subtilism Carlsberg; Subtilopeptidase A) is unfolded in the presence of 7 M guanidine hydrochloride. The unfolding reaches a maximum in approximately 6 min at 20C at pH 8.0. This is demonstrated by an increase of the mean residue ellipticity at 222 nm from -8.02 x 10-3 to -1.72 x 10-3 deg. cm-2/decimole. The unfolding is partially reversible and this reversibility is favoured by lower concentrations of enzyme. The fact that the refolding process is not complete may be attributed to either the demonstrated self association of the denatured enzyme or to interference of non-covalently bound autolysis peptides.

摘要

在7M盐酸胍存在的情况下，抑制性枯草杆菌蛋白酶（枯草杆菌蛋白酶卡尔伯格；枯草杆菌肽酶A）会发生去折叠。在20℃、pH值为8.0的条件下，去折叠过程在大约6分钟内达到最大值。这通过222nm处平均残基椭圆率从-8.02×10⁻³增加到-1.72×10⁻³度·厘米⁻²/ 十分之一摩尔得以证明。去折叠是部分可逆的，且较低浓度的酶有利于这种可逆性。再折叠过程不完全这一事实可能归因于已证明的变性酶的自我缔合或非共价结合的自溶肽的干扰。