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- W2041031738 abstract "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 μM. 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." @default.
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- W2041031738 date "2004-04-01" @default.
- W2041031738 modified "2023-09-23" @default.
- W2041031738 title "Adustin, a small translation-inhibiting polypeptide from fruiting bodies of the wild mushroom Polyporus adusta" @default.
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- W2041031738 doi "https://doi.org/10.1016/j.peptides.2004.01.021" @default.
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