Please use this identifier to cite or link to this item: http://nopr.niscair.res.in/handle/123456789/42647
Title: Conserved cysteine residues in malaria chorismate synthase indicate their important role in protein structure and function
Authors: Khera, Harvinder Kour
Singh, Susheel Kumar
Bhat, GN
Singh, Subhash
Keywords: Chorismate synthase;Cysteines;Disulfide linkages;Malaria;Plasmodium falciparum
Issue Date: Oct-2016
Publisher: NISCAIR-CSIR, India
Abstract: Predicted protein sequences of Chorismate synthase (Cs) from different Plasmodium species have shown high number of conserved cysteine residues when compared to the predicted Cs protein sequences from other bacterial, fungal or plant species. To better understand the structure and function of malaria Cs, we have cloned, expressed and purified recombinant Cs from Plasmodium falciparum (rPfCs) in E.coli. the rPfCs exhibited disulfide linkages as indicated by mobility shifts observed for this protein when compared between non-reduced and reduced-alkylated conditions on SDS-PAGE. Antibodies generated against rPfCs also detected similar mobility shift for the native parasite protein from asexual blood stage culture indicating that the conserved cysteine residues in native parasite Cs play an important role in the protein structure and function.
Page(s): 161-168
URI: http://nopr.niscair.res.in/handle/123456789/42647
ISSN: 0975-0959 (Online); 0301-1208 (Print)
Appears in Collections:IJBB Vol.53(5&6) [October-December 2016]

Files in This Item:
File Description SizeFormat 
IJBB 53(5&6) 161-168.pdf412.93 kBAdobe PDFView/Open


Items in NOPR are protected by copyright, with all rights reserved, unless otherwise indicated.