Purification and properties of a DNA ligase from sea urchin embryos.
スポンサーリンク
概要
- 論文の詳細を見る
DNA ligase was purified about 2, 000-fold from blastulae of sea urchin, Hemicentrotus pulcherrimus, by means of 1M KCl-extraction, phosphocellulose, DEAE-cellulose, Sepharose CL-6B, and double-stranded DNA cellulose column chromatography. The purified DNA ligase had a molecular weight of 80, 000 (determined by Sephadex G-150) and a sedimentation coefficient of 4.1 S (by glycerol gradient centrifugation). The purified enzyme required ATP and Mg2+ (or Mn2+) as cofactors for activity, and was inhibited by N-ethylmaleimide. Apparent Km values for ATP, Mg2+, and Mn2+ were 4 μM, 2.7mM, and 0.3mM, respectively.
- 社団法人 日本生化学会の論文
社団法人 日本生化学会 | 論文
- Role of Histidine 46 in the Hydrolysis and the Reverse Transphosphorylation Reaction of RNase Rh from Rhizopus niveus.
- Inhibition of Aspartate Chemotaxis of Escherichia coli by Site-Directed Sulfhydryl Modification of the Receptor.
- Characterization and Primary Structure of a Base Non-Specific and Acid Ribonuclease from Dictyostelium discoideum.
- BIOCHEMICAL STUDIES ON CARBOHYDRATES:XXXV. Chondrosin
- THE INFLUENCE OF INORGANIC IONS ON THE ACTIVITY OF AMYLASES