%0 Journal Article
%T Emerging Order of Species of Hirudin in Recombinant Pichia pastoris Fermentation
毕赤酵母发酵生产中的水蛭素降解顺序
%A YANG Ji-Zhong
%A ZHOU Xiang-Shan XIE Xi-Jun YOU Jin-Hua ZHANG Yuan-Xing
%A
杨继忠
%A 周祥山
%A 解锡军
%A 尤金花
%A 张元兴
%J 微生物学通报
%D 2004
%I
%X 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.
%K Pichia pastoris
%K Hirudin
%K Degradation
%K Cell-free extract
毕赤酵母
%K 水蛭素
%K 降解
%K 裂解液
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=78024727B5F4EF6AA9CA8E605B5FC464&aid=A0615A8F75462732&yid=D0E58B75BFD8E51C&vid=4AD960B5AD2D111A&iid=94C357A881DFC066&sid=B91E8C6D6FE990DB&eid=DB817633AA4F79B9&journal_id=0253-2654&journal_name=微生物学通报&referenced_num=3&reference_num=5