摘要
水蛭素 (rHV2 Lys4 7)是一个具有 65个氨基酸的抗凝活性肽。在毕赤酵母高密度发酵分泌表达过程中 ,发酵上清中可检出 4个水蛭素活性组份 ,分别为Hir65及其C 末端切除 1～ 3个氨基酸的Hir64、Hir63和Hir62。但目前 4种组份间的衍生关系还不清楚 ,以从发酵上清液中纯化分离所得的 4个组份作为底物 ,加入到菌体裂解液中 ,发现Hir64、Hir63和Hir62组份是由羧肽酶依次降解Hir65肽链C 末端 1个氨基酸后的产物。
Hirudin (rHV2-Lys 47) is a polypeptide of 65 amino acids, as the most potent and specific inhibitor of thrombin so far known. Four active fractions including the intact rHV2 (Hir65) and its three C-terminally truncated forms, Hir64, Hir63 and Hir62, were purified from the culture supernatant of Pichia pastoris. The emerging order of four species of hirudin was investigated by adding purified Hir65, Hir64 and Hir63 to cell-free extract respectively. Hir64, Hir63 and Hir62 were found to derive from Hir65 by truncating carboxy-terminal amino acid one by one by carboxypeptidase.
出处
《微生物学通报》
CAS
CSCD
北大核心
2004年第5期24-27,共4页
Microbiology China
关键词
毕赤酵母
水蛭素
降解
裂解液
Pichia pastoris, Hirudin, Degradation, Cell-free extract
