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Title of Journal: Biotechnol Lett

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Abbravation: Biotechnology Letters

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Springer Netherlands

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DOI

10.1002/chin.200244127

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1573-6776

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Purification of a recombinant histidinetagged lac

Authors: Balamurugan Sundaram Nandan Mysore Varadarajan Pradeep Annamalai Subramani Susanta Kumar Ghosh Viswanathan Arun Nagaraj
Publish Date: 2014/07/22
Volume: 36, Issue: 12, Pages: 2473-2480
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Abstract

Lactate dehydrogenase LDH of the malaria parasite Plasmodium vivax Pv serves as a drug target and immunodiagnostic marker The LDH cDNA generated from total RNA of a clinical isolate of the parasite was cloned into pRSETA plasmid Recombinant histagged PvLDH was overexpressed in E coli Rosetta2DE3pLysS and purified using Ni2+NTA resin giving a yield of 25–30 mg/litre bacterial culture The recombinant protein was enzymatically active and its catalytic efficiency for pyruvate was 54 × 108 min−1 M−1 145 fold higher than a low yield preparation reported earlier to obtain PvLDH crystal structure The enzyme activity was inhibited by gossypol and sodium oxamate The recombinant PvLDH was reactive in lateral flow immunochromatographic assays detecting pan and vivaxspecific LDH The soluble recombinant PvLDH purified using heterologous expression system can facilitate the generation of vivax LDHspecific monoclonals and the screening of chemical compound libraries for PvLDH inhibitorsThis study was supported by grants from Small Business Innovation Research Initiative Department of Biotechnology New Delhi BT/SBIRI/794/2B16/2011 and Science and Engineering Research Board Department of Science and Technology New Delhi SR/S2/RJN13/2010 VAN is a DST Ramanujan Fellow Thanks are due to Prof G Padmanaban and Prof P N Rangarajan for helpful discussions and providing the laboratory facilities

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