2016, Number 4

Journal of Animal and Poultry Sciences (JAPSC)

Vol 5(4), 2016

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Biochemical characterization of glutathione S-transferaases purified from chick embryo brain 

42-51

Dasari*, S. Gonuguntla, M. Ganjayi, B. Meriga, and Th. Kedam

 

Abstract

Glutathione-S-transferases (GSTs) are phase II defence enzymes and they use multi strategies to protect cellular system from both exogenous and endogenous noxious elements. So, researchers and pharmacologists’ are showing interest on GSTs from several decades. Generally birds are highly mobile in both earth and air, and they go through various environments polluted by either industrialization or crop system modernized with pesticide, herbicides and etc. But there is no sufficient attention on defence enzymatic system on birds. The present study was aimed to purify chick embryo brain cytosolic GSTs by using glutathione CL-agarose affinity matrices and the purified GSTs were showed significant activities with model substrates. In addition to that, chick embryo brain GST was exhibit glutathione dependent peroxidase activity. Affinity purified chick embryo brain GSTs were resolved into two bands on 12% sodium dodecyl sulphate polyacrylamide gel (SDS PAGE) and they named as CBI and CBII.  Biochemical characterization of GST was agreed with the previous literature. So, it was identified that the affinity purified brain GSTs from chick embryo may be related alpha and mu class.

 

Key words: Chick embryo barin, Glutathione CL-agarose affinity column, CBI & CBII, Alpha & Mu GSTs