Abstract
An antifungal protein, possessing a molecular weight of 28 kDa and an N-terminal sequence resembling chitinases, has been purified from the seeds of the field bean Dolichos lablab. The procedure involved extraction with aqueous buffer, affinity chromatography on Affi-gel blue gel, and ion exchange chromatography on CM-Sepharose. The protein, designated dolichin, exhibited antifungal activity against the fungi Fusarium oxysporum, Rhizoctonia solani, and Coprinus comatus. Dolichin was capable of inhibiting human immunodeficiency virus (HIV) reverse transcriptase and alpha- and beta-glucosidases which are glycohydrolases implicated in HIV infection. It had very low ribonuclease and cell-free translation-inhibitory activities.
Copyright 2000 Academic Press.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Anti-HIV Agents / chemistry
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Anti-HIV Agents / isolation & purification
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Anti-HIV 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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Chitinases / chemistry
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Chitinases / genetics
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Chitinases / isolation & purification
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Enzyme Inhibitors / chemistry
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Enzyme Inhibitors / isolation & purification
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Enzyme Inhibitors / pharmacology
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Fabaceae / chemistry*
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Fabaceae / genetics
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Fungi / drug effects
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Glucosidases / antagonists & inhibitors
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HIV Reverse Transcriptase / antagonists & inhibitors
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HIV-1 / drug effects
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HIV-1 / enzymology
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Humans
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Microbial Sensitivity Tests
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Molecular Sequence Data
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Plant Proteins / chemistry
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Plant Proteins / genetics
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Plant Proteins / isolation & purification*
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Plants, Medicinal*
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Seeds / chemistry
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Sequence Homology, Amino Acid
Substances
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Anti-HIV Agents
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Antifungal Agents
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Enzyme Inhibitors
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Plant Proteins
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HIV Reverse Transcriptase
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Glucosidases
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Chitinases