title: Purification of allivin, a novel antifungal protein from bulbs of the round-cloved garlic.
abstract: A novel antifungal protein, designated allivin, was isolated from bulbs of the round-cloved garlic Allium sativum var. round clove with a procedure involving ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-Sepharose and FPLC-gel filtration on Superdex 75. Allivin possessed an N-terminal sequence demonstrating very little similarity to sequences of Allium sativum chitinases and ribosome inactivating proteins. Allivin exhibited a molecular weight of 13 kDa in gel filtration and SDS-polyacrylamide gel electrophoresis. It displayed antifungal activity against Botrytis cinerea, Mycosphaerella arachidicola and Physalospora piricola. It inhibited translation in a cell-free rabbit reticulocyte system with an IC50 of 1.6 microM.
authors: Department of Microbiology, College of Biological Science, China Agricultural University, Beijing.
authors: H X
authors: HX
authors: Wang
authors: T B
authors: TB
authors: Ng
mesh_terms: D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000302:isolation & purification* / Q000494:pharmacology; D005737:Garlic / Q000737:chemistry*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology
chemical_list: D000935:Antifungal Agents; D010940:Plant Proteins; C454981:allivin protein, Allium sativum