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High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum

Hill, Jeffrey, Tyas, Lorraine, Phylip, Lowri H., Kay, John, Dunn, Ben M. and Berry, Colin 1994. High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum. FEBS Letters 352 (2) , pp. 155-158. 10.1016/0014-5793(94)00940-6

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Abstract

DNA encoding the last 48 residues of the propart and the whole mature sequence of Plasmepsin II was inserted into the T7 dependent vector pET 3a for expression in E. coli. The resultant product was insoluble but accumulated at ∼20 mg/l of cell culture. Following solubilisation with urea, the zymogen was refolded and, after purification by ion-exchange chromatography, was autoactivated to generate mature Plasmepsin II. The ability of this enzyme to hydrolyse several chromogenic peptide substrates was examined; despite an overall identity of ∼35% to human renin, Plasmepsin II was not inhibited significantly by renin inhibitors.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Biosciences
ISSN: 0014-5793
Last Modified: 20 Dec 2017 01:53
URI: http://orca.cf.ac.uk/id/eprint/64829

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