Chang J Y
Pharmaceuticals Research Laboratory, Ciba-Geigy Ltd., Basel, Switzerland.
Biochem J. 1994 Jun 15;300 ( Pt 3)(Pt 3):643-50. doi: 10.1042/bj3000643.
The folding of hirudin undergoes an initial stage of non-specific packing, followed by consolidation (re-organization) of partially packed intermediates to attain the native structure [Chatrenet and Chang (1993) J. Biol. Chem. 268, 20988-20996]. Non-specific packing leads to the formation of scrambled hirudins as folding intermediates. A systematic study was carried out to search for conditions which would selectively control and enhance the processes of packing and consolidation. It is demonstrated here that under optimized conditions, including the use of cystine/cysteine and protein disulphide isomerase, the folding of hirudin in vitro can be achieved quantitatively within 30 s.
水蛭素的折叠经历一个非特异性堆积的初始阶段,随后是部分堆积中间体的巩固(重新组织)以达到天然结构[Chatrenet和Chang(1993年)《生物化学杂志》268卷,20988 - 20996页]。非特异性堆积导致形成作为折叠中间体的混乱水蛭素。进行了一项系统研究以寻找能够选择性控制和增强堆积与巩固过程的条件。此处证明,在优化条件下,包括使用胱氨酸/半胱氨酸和蛋白质二硫键异构酶,水蛭素在体外的折叠可在30秒内定量完成。