Academic Journals Database
Disseminating quality controlled scientific knowledge

Purification of Mutarotase, Extracted from Bovine Kidney Cortex

ADD TO MY LIST
 
Author(s): M. Anjum Zia | Khalil-ur-Rehman | Nadia Jamil | Farzana Alyas

Journal: Biotechnology
ISSN 1682-296X

Volume: 2;
Issue: 2;
Start page: 109;
Date: 2003;
VIEW PDF   PDF DOWNLOAD PDF   Download PDF Original page

Keywords: Mutarotase | kidney | purification | polarimeter

ABSTRACT
Bovine kidney cortex was homogenized to extract mutarotase that was subjected to ammonium sulfate precipitation, ion exchange and gel filtration chromatographic techniques. The activity and specific activity of crude enzyme was observed as 1.27 and 0.34 U mg-1, respectively which was increased by 3.52 and 2.55 U mg-1 after partial purification by ammonium sulfate precipitation and desalting. The enzyme was then subjected to DEAE column for ion exchange chromatography and the resultant activity and specific activity gained by the enzyme was 3.17 and 2.50 U mg-1, respectively. After gel filtration chromatography through sephadex G-150, the observed activity and specific activity was 2.894 and 3.36 U mg-1 which indicates 9.97 fold purification.
Affiliate Program     

Tango Jona
Tangokurs Rapperswil-Jona