Streptomyces lavendulaeProtease Inhibitor: Purification, Gene Overexpression, and 3-Dimensional Structure

Author:

El-Hadedy D. E.1,Mostafa El-Sayed E.2,Saad Moataza M.2

Affiliation:

1. Microbiology Department, National Center for Radiation Research and Technology (NCRRT), 3 Ahmed El-Zomor Street, 8th Sector, Nasr City, Cairo 11371, Egypt

2. Microbial Chemistry Department, National Research Centre (NRC), El-Bohouth Street, P.O. Box 12622, Dokki, Cairo, Egypt

Abstract

Protease inhibitorstrypsin (STI1, Streptomyces trypsin inhibitor 1) has been identified, purified by ammonium sulfate precipitation and Sephadex G-100 gel filtration. SDS-PAGE of protease inhibitor showed molecular weight of approximately 10 KDa. PCR product (~1615 bp) ofsti1gene was cloned in expression vectorpACYC177/ET3dand transformed inEscherichia coliJM109.Protease inhibitorstrypsin was purified and used as antivirus against Coxsackievirus B3 (CVB3). CVB3 is one of the major causative agents of chronic, subacute, acute, and fulminant myocarditis as well as pancreatitis and aseptic meningitis. It has been reported that more than 50% of human myocarditis is associated with CVB3 infection.

Publisher

Hindawi Limited

Subject

General Chemistry

Cited by 1 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献

1. Microbial serine protease inhibitors and their therapeutic applications;International Journal of Biological Macromolecules;2018-02

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