Cloning and activity analysis of a new protease from Arenicola cristata

摘要

The protease gene Arenicola cristata was cloned, sequenced, and expressed in E.coli and the activity of the recombinant protein was investigated. The full-length cDNA of 880 bp consisted of an ORF of 813bp encoding 270 amino acids. This protease contained highly conserved GDSGGP sequence and revealed high homology with trypsin-like proteases of serine family. The recombinant protein for the active form of the protease was purified by affinity chromatography. The activity analysis of the recombinant protein suggested that it was probably a plasminogen activator.