title: Sativin: a novel antifungal miraculin-like protein isolated from legumes of the sugar snap Pisum sativum var. macrocarpon.
abstract: 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.
authors.affiliation: Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories.
authors.forename: X Y
authors.initials: XY
authors.lastname: Ye
authors.forename: H X
authors.initials: HX
authors.lastname: Wang
authors.forename: T B
authors.initials: TB
authors.lastname: Ng
mesh_terms: 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
chemical_list: D000935:Antifungal Agents; D010940:Plant Proteins; C412782:sativin protein, Pisum sativum