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Purification and properties of suppressor seryl‐tRNA:ATP phosphotransferase from bovine liver
Author(s) -
Mizutani Takaharu,
Hashimoto Atsushi
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80342-7
Subject(s) - biochemistry , phosphotransferase , aminoacyl trna synthetase , chemistry , transfer rna , suppressor , biology , microbiology and biotechnology , enzyme , rna , gene
Seryl‐tRNA Ser CmCA :ATP phosphotransferase was purified 1200‐fold from bovine liver by ultracentrifugation at 150 000 × g , chromatography on DEAE—cellulose, fractional precipitation with ammonium sulfate, chromatography on hydroxyapatite, gel filtration on Sephacryl S‐300 and affinity chromatography on Blue Sepharose. Molecular mass was estimated as 135–145 kDa. The K m values for ATP and ser‐tRNA Ser CmCA were 2 mM and 21 nM, respectively. This enzyme did not react with ser‐tRNA Ser IGA , tyr‐tRNA or thr‐tRNA.