Alocasin, an anti-fungal protein from rhizomes of the giant taro Alocasia macrorrhiza.
An anti-fungal protein designated alocasin was isolated from the rhizomes of the giant taro Alocasia macrorrhiza. The isolation protocol involved ion exchange chromatography on diethylaminoethyl (DEAE)-cellulose, ion exchange chromatography on sulfopropyl (SP)-Sepharose, and gel filtration on Superdex 75. Alocasin, which was unadsorbed on DEAE-cellulose and SP-Sepharose, possessed the N-terminal sequence APEGEV, which exhibited some similarity to that of the miraculin-like anti-fungal protein from Pisum sativum legumes. It demonstrated a molecular mass of 11kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, and displayed anti-fungal activity against Botrytis cinerea. Alocasin reduced the activity of HIV-1 reverse transcriptase. It exhibited weak hemagglutinating activity, only at a concentration of 1mg/ml.
Wang
H X
HX
Department of Microbiology, College of Biological Science, China Agricultural University, Beijing, China.
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TB
D031055:Alocasia / Q000737:chemistry*; D000595:Amino Acid Sequence; D000935:Antifungal Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D008969:Molecular Sequence Data; D028321:Plant Preparations / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology*; D018894:Reverse Transcriptase Inhibitors / Q000494:pharmacology; D027343:Rhizome / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D000935:Antifungal Agents; D028321:Plant Preparations; D010940:Plant Proteins; D018894:Reverse Transcriptase Inhibitors