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Journal of Medical Sciences

Year: 2001  |  Volume: 1  |  Issue: 6  |  Page No.: 404 - 406

Partial Purification of Peroxidase from Tomato

M. Anjum Zia, Khalil-ur-Rehman, M. Khalid Saeed, Aftab Ahmed and Abdul Ghaffar

Abstract

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.

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