Abstract
A novel single-chained antifungal protein with a molecular weight of 13 kDa displaying an N-terminal sequence with marked similarity to embryo-abundant protein from the white spruce was isolated from the seeds of Ginkgo biloba using ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on SP-Sepharose, and then gel filtration on Superdex 75. The protein, designated ginkbilobin, exerted potent antifungal activity against a variety of fungi, including Botrytis cinerea, Mycosphaerella arachidicola, Fusarium oxysporum, Rhizoctonia solani, and Coprinus comatus. Ginkbilobin exhibited a moderate antibacterial action against Staphylococcus aureus, Pseudomonas aeruginosa, and Escherichia coli. It suppressed the activity of HIV-1 reverse transcriptase and the proliferation of murine splenocytes.
Copyright 2000 Academic Press.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Anti-Bacterial Agents
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Anti-Infective Agents / chemistry*
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Anti-Infective Agents / isolation & purification
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Anti-Infective Agents / pharmacology
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Antifungal Agents / chemistry*
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Antifungal Agents / isolation & purification
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Antifungal Agents / pharmacology
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Bacteria / drug effects*
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Cell Division / drug effects
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Chromatography, Affinity
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Chromatography, Gel
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Chromatography, Ion Exchange
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Fungi / classification
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Fungi / drug effects*
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Ginkgo biloba*
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HIV-1 / enzymology
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Lymphocytes / cytology
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Lymphocytes / drug effects
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Mice
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Mice, Inbred C57BL
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Microbial Sensitivity Tests
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Plant Proteins / chemistry*
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Plant Proteins / isolation & purification
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Plant Proteins / pharmacology
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Plants, Medicinal*
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Reverse Transcriptase Inhibitors / pharmacology
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Seeds
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Spleen / cytology
Substances
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Anti-Bacterial Agents
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Anti-Infective Agents
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Antifungal Agents
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Plant Proteins
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Reverse Transcriptase Inhibitors
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ginkbilobin protein, Ginkgo biloba