Biochemical characterization of casein kinases II from chloroplasts of spinach, Spinacia oleracea

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概要

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• Monomeric (38kDa) and oligomeric (140kDa) forms of casein kinase II (CK-II) were partially purified from spinach chloroplasts by heparin-agarose column chromatography and gel filtration on Superdex 200 pg (HPLC). The enzymatic properties [requirements of phosphate acceptors and phosphate donors (ATP and GTP), and sensitivity to heparin] of the two kinases exactly corresponded to those reported for various animal CK-IIs. Although poly-Lys and spermine (activators for animal CK-II) stimulated the activity of oligomeric CK-II, no significant effect of these activators on the phosphorylation of casein by monomeric CK-II was detected. Moreover, it has been shown that monomeric CK-II is main form in spinach chloroplasts.

著者

• KANEKATSU Motoki

  Laboratory of Biology, School of Liberal Arts and Sciences, Kitasato University

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.

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