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Original scientific paper

Expression and purification of the major outer membrane protein (OmpH) of Pasteurella multocida P52 from Escherichia coli

Rashmi Singh ; Department of Veterinary Microbiology, College of Veterinary and Animal Sciences, Govind Ballabh Pant University of Agriculture and Technology, Pantnagar, Uttarakhand, India
Praveen Kumar Gupta ; Division of Veterinary Biotechnology, Indian Veterinary Research Institute, Izatnagar, India
Velagapudi Durga Prasad Rao ; Department of Veterinary Microbiology, College of Veterinary and Animal Sciences, Govind Ballabh Pant University of Agriculture and Technology, Pantnagar, Uttarakhand, India


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Abstract

Porin H (OmpH) is the major outer membrane protein in the envelope of Pasteurella multocida. The gene ompH, encoding major outer membrane protein was amplified by PCR excluding the region coding for signal peptide and cloned in the pQE32 prokaryotic expression vector. The recombinant OmpH was expressed as a fusion protein with 6-His tag at N-terminal in E. coli M15 cells transformed with recombinant plasmid pQE32-ompH. The expressed protein was purified from E. coli and characterized by SDS-PAGE and western blot analysis. The fusion recombinant protein eluted had a molecular mass of about 37 kDa. The expressed recombinant protein was confirmed with western blot analysis using RGS-His antibody and anti-P. multocida serum raised against whole cell lysate.

Keywords

haemorrhagic septicaemia; outer membrane protein; Pasteurella multocida; recombinant protein

Hrčak ID:

53087

URI

https://hrcak.srce.hr/53087

Publication date:

18.12.2009.

Article data in other languages: croatian

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