Purification and subunit structure of phenylalanyl-tRNA synthetase from hen liver mitochondria |
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Authors: | Hans-Joachim Gabius Friedrich Cramer |
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Institution: | Max-Planck-Institut für experimentelle Medizin, Abteilung Chemie Hermann-Rein-Straße 3, D-3400 Göttingen, Federal Republic of Germany |
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Abstract: | Hen liver mitochondrial phenylalanyl-tRNA synthetase is purified to homogeneity by a series of steps including salting-out chromatography, salting-out affinity chromatography in the presence of tRNAPhe, dissociation of the enzyme-tRNA complex on DEAE-cellulose, chromatography on DEAE-Sepharose CL-6B and Sepharose 6B. The enzyme appears to be a tetrameric enzyme with a molecular weight of 255 000, as determined by gel filtration, with a subunit structure of α2β2 (α = 57 000, β = 66 000), as determined by sodium dodecyl sulfate gel electrophoresis. |
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