Journal article
Authors list: Färber, PM; Arscott, LD; Williams, CH; Becker, K; Schirmer, RH
Publication year: 1998
Pages: 311-314
Journal: FEBS Letters
Volume number: 422
Issue number: 3
ISSN: 0014-5793
DOI Link: https://doi.org/10.1016/S0014-5793(98)00031-3
Publisher: Wiley
Abstract:
Plasmodium falciparum glutathione reductase (PfGR) has emerged as a drug target against tropical malaria, Here me report the expression of PfGR in Escherichia coli SG5(DE3) and isolation procedures for this protein. Recombinant PfGR does not differ from the authentic enzyme in its enzymic properties, the turnover number being 9900 min(-1), The dimeric flavoenzyme exhibits redox-dependent absorption spectra; the single tryptophan residue (per 57.2 kDa subunit) is strongly fluorescent. PfGR can be inhibited by the antimalarial drug methylene blue at therapeutic concentrations; the K-i for non-competitive inhibition is 6.4 mu M. The sensitivity to methylene blue is observed also at high ionic strength so that, by analogy to human GR, analysis of crystalline enzyme-drug complexes can be envisaged. (C) 1998 Federation of European Biochemical Societies.
Citation Styles
Harvard Citation style: Färber, P., Arscott, L., Williams, C., Becker, K. and Schirmer, R. (1998) Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue, FEBS Letters, 422(3), pp. 311-314. https://doi.org/10.1016/S0014-5793(98)00031-3
APA Citation style: Färber, P., Arscott, L., Williams, C., Becker, K., & Schirmer, R. (1998). Recombinant Plasmodium falciparum glutathione reductase is inhibited by the antimalarial dye methylene blue. FEBS Letters. 422(3), 311-314. https://doi.org/10.1016/S0014-5793(98)00031-3