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- W2167767404 abstract "We have purified proteasomes to apparent homogeneity from the archaebacterium Thermoplasma acidophilum . This proteinase has a molecular mass of about 650 kDa and an isoelectric point of 5.6. The proteasome hydrolyses peptide substrates containing an aromatic residue adjacent to the reporter group, as well as [ 14 C]methylated casein optimally at pH 8.5 and 90°C. The enzyme activity is enhanced severalford by Mg 2+ and Ca 2+ at 25–500 mM. This increase in activity results primarily from a change in K m . The serine‐proteinase inhibitors diisopropylfluorophosphate and 3,4‐dichlorosiocoumarin irreversibly inhibit the enzyme, obviously by modification of both the α and β subunits in the proteasome. The inhibition of proteasomal activity by the peptidylchloromethanes, Cbz‐Leu‐Leu‐CH 2 Cl and Cbz‐Ala‐Ala‐Phe‐Ch 2 Cl (Cbz, benzyloxycarbonyl), is reversible and predominantly of a competitive type. The enzyme is not activated by any of the compounds that typically stimulate the activities of the eukaryotic proteasome." @default.
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- W2167767404 date "1992-09-01" @default.
- W2167767404 modified "2023-10-17" @default.
- W2167767404 title "Biochemical properties of the proteasome from <i>Thermoplasma acidophilum</i>" @default.
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- W2167767404 doi "https://doi.org/10.1111/j.1432-1033.1992.tb17249.x" @default.
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