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2000
Volume 18, Issue 6
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

A 7.3-kDa antifungal peptide was purified from dried red kidney beans. The purification procedure entailed ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-cellulose, followed by fast protein liquid chromatography-gel filtration on Superdex 75. The peptide was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and CM-cellulose. It exhibited a molecular mass of 7.3 kDa in gel filtration and also in SDS-polyacrylamide gel electrophoresis, indicating that it is a single-chained protein. The N-terminal sequence of the peptide was DGVCFGGLANGDRT. The peptide exerted an antifungal action on Fusarium oxysporum with an IC50 of 3.8±0.4 μM (mean±SD, n=3). It also inhibited mycelial growth in Mycosphaerella arachidicola. It suppressed growth of lymphoma MBL2 cells and leukemia L1210 cells with an IC50 of 5.2±0.4 μM and 7.6±0.6 μM, respectively. HIV-1 reverse transcriptase was inhibited with an IC50 of 40±3.2 μM. However, no activity was demonstrated toward other viral enzymes.

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/content/journals/ppl/10.2174/092986611795222803
2011-06-01
2025-09-04
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/content/journals/ppl/10.2174/092986611795222803
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  • Article Type:
    Research Article
Keyword(s): antifungal; antiproliferative; characterization; HIV-1; leguminous seeds; Purification
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