Purification of a 34 kDa ribonucleoprotein (p34) from spinach chloroplasts as an effective phosphate acceptor for casein kinase II.
スポンサーリンク
概要
- 論文の詳細を見る
A 34kDa ribonucleoprotein (p34) was purified to homogeneity from a 1.0M KCl extract of spinach chloroplasts as an effective phosphate acceptor for casein kinase II (CK-II) by means of heparin-agarose, DEAE-cellulose, Sephacryl S300, dsDNA-cellulose and Mono Q column chromatography. Biochemical analysis of purified p34 show that the native form of p34 is a monomeric protein and p34 is phosphorylated specifically by CK-II in the chloroplasts.
- 日本学士院の論文
著者
関連論文
- Chloroplast Ribonucleoproteins (RNPs) as Phosphate Acceptors for Casein Kinase II : Purification by ssDNA-Cellulose Column Chromatography : PROTEINS, ENZYMES AND METABOLISM
- Biochemical characterization of casein kinases II from chloroplasts of spinach, Spinacia oleracea
- The effects of nucleic acids on the casein kinase II catalyzed phosphorylation of a 34kDa ribonucleoprotein purified from spinach chloroplasts
- Purification of a 34 kDa ribonucleoprotein (p34) from spinach chloroplasts as an effective phosphate acceptor for casein kinase II.