Purification and characterization of a glycoprotein inhibitor of toxic phospholipase from Withania somnifera

Deepa, M. and Veerabasappa Gowda, T. (2002) Purification and characterization of a glycoprotein inhibitor of toxic phospholipase from Withania somnifera. Archives of Biochemistry and Biophysics, 408 (1). 42 - 50. ISSN 1096-0384

Full text not available from this repository. (Request a copy)
Official URL: https://doi.org/10.1016/S0003-9861(02)00527-1

Abstract

A phospholipase inhibitor (WSG) has been purified from Withania somnifera using gel-filtration and ion-exchange chromatographies. The WSG is an acidic glycoprotein. Its molecular mass as determined by SDS–PAGE was 27kDa. It neutralized the enzyme activity and pharmacological properties such as cytotoxicity, edema, and myotoxicity of a multi-toxic Indian cobra venom phospholipase (NNXIa–PLA) but failed to neutralize the neurotoxicity. The glycan part of the molecule does not appear to be involved in any of the pharmacological properties studied. The results suggest that the neutralization of the pharmacological effects of the toxic phospholipase is brought about by inhibition of the enzyme activity by formation of a complex between the WSG and the toxic phospholipase. We report the purification and characterization of a glycoprotein phospholipase A inhibitor from Withania somnifera, medicinal plant.

Item Type: Article
Uncontrolled Keywords: , Phospholipase A inhibitor, Antimyotoxic, Glycoprotein, venom
Subjects: C Chemical Science > Biochemistry
Divisions: Department of > Biochemistry
Depositing User: Manjula P Library Assistant
Date Deposited: 20 Sep 2019 05:37
Last Modified: 20 Sep 2019 05:37
URI: http://eprints.uni-mysore.ac.in/id/eprint/8292

Actions (login required)

View Item View Item