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Title 

Molecular cloning, sequencing, and expression of a fibrinolytic serine-protease gene from the earthworm Lumbricus rubellus

Authors 

I H ChoEui Sung ChoiH H Lee

Publisher 

Springer Verlag (Germany)

Issue Date 

2004

Citation 

Journal of Biochemistry and Molecular Biology, vol. 37, no. 5, pp. 574-581

Keywords 

gene cloninglumbricus rubelluslumbrokinaseproteaseescherichia colipheretima sieboldifibrinolytic agentserine proteinaseamino acid sequence

Abstract 

The full-length cDNA of the lumbrokinase fraction 6 (F6) protease gene of Lumbricus rubellus was amplified using an mRNA template, sequenced and expressed in E. coli cells. The F6 protease gene consisted of pro- and mature sequences by gene sequence analysis, and the protease was translated and modified into active mature polypeptide by N-terminal amino acid sequence analysis of the F6 protease. The pro-region of F6 protease consisted of the 44 residues from methionine-1 to lysine-44, and the mature polypeptide sequence (239 amino acid residues and one stop codon; 720 bp) started from isoleucine-45 and continued to the terminal residue. F6 protease gene clones having pro-mature sequence and mature sequence produced inclusion bodies in E. coli cells. When inclusion bodies were orally administrated rats, generated thrombus weight in the rat's venous was reduced by approximately 60% versus controls. When the inclusion bodies were solubilized in pepsin and/or trypsin solutions, the solubilized enzymes showed hemolytic activity in vitro. It was concluded the F6 protease has hemolytic activity, and that it is composed of pro- and mature regions.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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