title: Expression and characterization of earthworm Eisenia foetida lumbrokinase-3 in Pichia pastoris.
abstract: Lumbrokinase-3 (LK-3, AY438622), first cloned from the earthworm Eisenia foetida in our laboratory, is a component of earthworm fibrinolytic enzymes. In this study, cDNA encoding the LK-3 gene was sub-cloned into yeast pPIC9K expression vector and transformed into the Pichia pastoris GS115 cells by electroporation. High level expression of LK-3 in yeast cells was confirmed with a different induction time. The activity of expressed LK-3 was observed in fibrin plates. In addition, the expressed LK-3 protein could dissolve fibrinogen and bovine serum albumin. The use of this system for the high level production of biological protein is implicated from this study.
authors.affiliation: Department of Pathophysiology, Beijing Institute of Radiation Medicine, Beijing, P. R. China.
authors.forename: Xiaoling
authors.initials: X
authors.lastname: Yuan
authors.forename: Chenhua
authors.initials: C
authors.lastname: Cao
authors.forename: Yajun
authors.initials: Y
authors.lastname: Shan
authors.forename: Zhenhu
authors.initials: Z
authors.lastname: Zhao
authors.forename: Jiapei
authors.initials: J
authors.lastname: Chen
authors.forename: Yuwen
authors.initials: Y
authors.lastname: Cong
mesh_terms: D000818:Animals; D010450:Endopeptidases / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism*; D015870:Gene Expression; D009835:Oligochaeta / Q000201:enzymology*; D010843:Pichia / Q000235:genetics; D011994:Recombinant Proteins / Q000096:biosynthesis* / Q000235:genetics / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D010450:Endopeptidases; C083421:lumbrokinase