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- W2067032001 abstract "Abstract Prenyltransferase (EC 2.5.1.1) has been purified to homogeniety from pig liver. The protein, which has been shown to be homogeneous by electrophoresis under several conditions, has a specific activity fourfold greater than that of previous preparations from this tissue. The protein is a dimer of molecular weight of approximately 80,000 whose subunits were not resolved by electrophoresis in sodium dodecyl sulfate. Michaelis constants for geranyl pyrophosphate and isopentenyl pyrophosphate were determined to be 0.58 and 0.31 μ m , respectively. The homogeneous enzyme could be resolved into two forms by isoelectric focusing or chromatography on DE-52 cellulose under certain conditions. The isoelectric points of the two forms were 4.85 and 4.99. The two forms of the enzyme were interconvertible and probably result from a slow equilibrium between two conformational isomers of the protein." @default.
- W2067032001 created "2016-06-24" @default.
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- W2067032001 date "1977-10-01" @default.
- W2067032001 modified "2023-10-17" @default.
- W2067032001 title "Purification and properties of pig liver prenyltransferase: Interconvertible forms of the enzyme" @default.
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- W2067032001 doi "https://doi.org/10.1016/0003-9861(77)90405-2" @default.
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