二硫键对毕赤酵母表达重组人复合
α干扰素的降解与聚合影响

Effect of Disulfide Bond on Degradation and Aggregation of Consensus Interferon-α Expressed by Pichia Pastoris

摘要: 毕赤酵母(Pichia pastoris)表达重组人复合α干扰素（cIFN）时会形成cIFN分子内二硫键异构体，cIFN发生强烈的降解、聚合等不均一表达现象。体外试验证实了cIFN的3种二硫键异构体，研究了形成不同二硫键异构体的条件和各自的稳定性，包括降解与聚合。当cIFN分子内部二硫键破裂时会对其稳定性造成致命影响，从而使cIFN更容易遭到发酵液中蛋白酶降解和聚合。

Abstract: When Consensus Interferon(cIFN) was expressed by Pichia pastoris, cIFN formatted intramolecular disulfidebond isomers. The phenomena of degradation and aggregation occurred seriously. Three disulfide isomers of cIFN were confined in vitro tests. The formation conditions and the stability of different disulfide isomers were investigated. The results showed that the intramolecular disulfide-bond of cIFN were responded to its stability, so as to make cIFN more easily to be encountered the degradation by the protease in the broth and to be induced to formatted aggregates.