摘要
天然二硫键的形成是许多蛋白正确折叠中的限速步骤,在稳定蛋白质构象和保持蛋白质 活性方面起重要作用。讨论的二硫键异构酶是内质网中一种重要的蛋白折叠催化剂,它催化蛋 白二硫键的形成和错误配对二硫键的重排,并有抑制错误折叠蛋白聚集的分子伴侣活性。PDI 广泛应用于基因工程上提高外源蛋白表达水平。
The formation of native disulfide bond is critical for the proper folding of many proteins. It maintains the integrity of protein structure and activity. This review focuses on one of important protein folding assistants- protein disulfide isomerase in endoplasmic reticulum. PDI, an enzyme that catalyzes disulfide formation and rearrangement of incorrect disulfide, behaves as a chaperone inhabiting the aggregation of misfolded proteins. It has a wide application in the expression of heterlogous proteins in eukaryotic hosts.
出处
《中国生物工程杂志》
CAS
CSCD
北大核心
2005年第B04期176-179,共4页
China Biotechnology
基金
国家重大科技专项(2002AA2Z345B)
