RENATURATION OF RECOMBINANT SECRETORY LEUKOCYTE PROTEASE INHIBITOR - ASPECTS OF DISULFIDE BOND FORMATION KINETICS

被引:6
作者
HARCUM, SW
DALE, BE
SEELY, RJ
机构
[1] COLORADO STATE UNIV,DEPT AGR & CHEM ENGN,FT COLLINS,CO 80523
[2] SYNERGEN INC,BOULDER,CO 80301
关键词
D O I
10.1007/BF00131761
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Therapeutic proteins produced in procaryotic hosts often contain disulfide bonds, which must be fully formed to satisfy United States Food and Drug Administration regulations. Native secretory leukocyte protease inhibitor (SLPI), a possible emphysema therapeutic agent, contains many disulfide bonds. However, when SLPI is produced in Escherichia coli by rDNA technology, the disulfide bonds are not formed correctly and must be generated by in vitro renaturation. In this study, the reaction rate parameters were estimated for SLPI renaturation. The apparent activation energy was approximately 5 kcal/mol suggesting that renaturation is a diffusion limited process. Apparent reaction rate orders were not constant, suggesting complex renaturation mechanism(s).
引用
收藏
页码:943 / 948
页数:6
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