Adustin, a small translation-inhibiting polypeptide from fruiting bodies of the wild mushroom Polyporus adusta.
A polypeptide, with a molecular mass of 16.5 kDa as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, has been isolated from the mushroom Polyporus adusta. The polypeptide, designated as adustin, inhibited translation in a cell-free rabbit reticulocyte lysate system with an IC50 of 0.34 microM. It was isolated using a protocol that involved ion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion exchange chromatography on CM-Sepharose and fast protein liquid chromatography-gel filtration on Superdex 75. Adustin was unadsorbed on DEAE-cellulose, and adsorbed on Affi-gel blue gel and CM-Sepharose.
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Department of Biochemistry, Faculty of Medicine, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, PR China. biochemistry@cuhk.edu.hk
Wang
Hexiang
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D000818:Animals; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000737:chemistry* / Q000302:isolation & purification* / Q000494:pharmacology; D005658:Fungi; D008970:Molecular Weight; D014176:Protein Biosynthesis / Q000187:drug effects*; D011817:Rabbits
D005656:Fungal Proteins; C496355:adustin, Polyporus adusta