Submit Manuscript

Journal of Medical Sciences

Year: 2001 | Volume: 1 | Issue: 6 | Page No.: 404-406
Facebook Twitter Digg Reddit Linkedin StumbleUpon E-mail

Article Trend

Total views 346

Search

Authors

M. Anjum Zia

Khalil-ur-Rehman

M. Khalid Saeed

Aftab Ahmed

Abdul Ghaffar

Keywords

Peroxidase from tomato was extracted and partially purified by means of ammonium sulphate [(NH4)2SO4] precipitation technique and ion exchange chromatography. The crude extract having the specific activity of 0.239U mg-1 was subjected to (NH4)2SO4 precipitation technique for partial purification of peroxidase. The specific activity of (NH4)2SO4 precipitated enzyme was 0.546U mg-1 with protein contents of 0.412mg ml-1. After ion exchange chromatography through DEAE-Cellulose columns, the specific activity was 11.844U mg-1 and the protein contents were decreased to 0.0358mg ml-1 showing that unnecessary proteins have been eliminated. Finally, partially purified enzyme was subjected to SDS-Electrophoresis for confirming the purification. So it was concluded that crude and partially purified enzymes from tomato possess an appreciable enzyme activity.
PDF Fulltext XML References Citation

Leave a Comment

Your email address will not be published. Required fields are marked *