Purification and subunit structure of mitochondrial phenylalanyl-tRNA synthetase from yeast
| Autor: | A.J.C. Stahl, M. Diatewa |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
Gel electrophoresis
Ammonium sulfate Chromatography Molecular mass biology Macromolecular Substances Protein subunit Saccharomyces cerevisiae Biophysics Cell Biology biology.organism_classification Biochemistry Yeast Mitochondria Amino Acyl-tRNA Synthetases Molecular Weight Phenylalanine—tRNA ligase chemistry.chemical_compound chemistry Sephadex Phenylalanine-tRNA Ligase Molecular Biology |
| Zdroj: | Biochemical and Biophysical Research Communications. 94:189-198 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/s0006-291x(80)80205-1 |
| Popis: | Summary Yeast mitochondrial Phe-tRNA synthetase is purified about 380-fold to homogeneity by precipitation with ammonium sulfate and chromatography on DEAE-cellulose, on two hydroxylapatite and on two AH-Sepharose 4B columns. The yield is 17%. The molecular weight is 266,000 as determined by Sephadex G-200 chromatography. The enzyme presents two types of subunits with molecular weights of 57000 and 72000, respectively, determined by urea-sodium dodecylsulfate gel electrophoresis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|