Sativin: a novel antifungal miraculin-like protein isolated from legumes of the sugar snap Pisum sativum var. macrocarpon.
An antifungal protein designated sativin was isolated from the legumes of the sugar snap (also known as honey pea) Pisum sativum var. macrocarpon. The procedure entailed extraction, affinity chromatography on Affi-gel blue gel and ion exchange chromatography on CM-Sepharose. The protein exhibited a molecular weight of 38 kDa in SDS-polyacrylamide gel electrophoresis. It possessed an N-terminal amino acid sequence which showed similarity to those of miraculin (a sweet protein) and pisavin (a ribosome-inactivating protein from Pisum sativum var arvense Poir manifesting similarity to miraculin). Unlike pisavin, however, sativin demonstrated negligible ribonuclease activity and inhibited translation in a rabbit reticulocyte lysate system with a very low potency (IC50= 14 microM). Sativin exerted antifungal activity against Fusarium oxysporum, Coprinus comatus and Pleurotus ostreatus but not against Rhizoctonia solani.
Ye
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Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories.
Wang
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HX
Ng
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TB
D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000302:isolation & purification / Q000494:pharmacology*; D002846:Chromatography, Affinity; D005658:Fungi / Q000187:drug effects / Q000254:growth & development; D020128:Inhibitory Concentration 50; D008969:Molecular Sequence Data; D018532:Pisum sativum / Q000737:chemistry*; D010940:Plant Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D012270:Ribosomes / Q000187:drug effects; D012639:Seeds / Q000737:chemistry; D017386:Sequence Homology, Amino Acid
D000935:Antifungal Agents; D010940:Plant Proteins; C412782:sativin protein, Pisum sativum