Cloning and Activity Analysis of a New Protease from Arenicola cristata

Ji Yu Ju; Jin Xin Chu; Chun Ling Zhao

doi:10.4028/www.scientific.net/AMR.998-999.206

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HomeAdvanced Materials ResearchAdvanced Materials Research Vols. 998-999Cloning and Activity Analysis of a New Protease...

Cloning and Activity Analysis of a New Protease from Arenicola cristata

Abstract:

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.

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Periodical:

Advanced Materials Research (Volumes 998-999)

Pages:

206-209

DOI:

https://doi.org/10.4028/www.scientific.net/AMR.998-999.206

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Online since:

July 2014

Authors:

Ji Yu Ju, Jin Xin Chu, Chun Ling Zhao*

Keywords:

Arenicola cristata, Fibrinolytic Activity, Molecular Cloning, Protease

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* - Corresponding Author

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