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- W2067844128 abstract "Chromatin subunits from murine erythroleukemia cells were prepared by a method which releases actively transcribing genes. Two casein kinase activities (CK 1 and CK 2 ) were isolated from these nucleosomes by gel nitration in 0.5 m NaCl. CK 1 ( M r ~ 200,000) and CK 2 ( M r ~ 35,000) were further purified by phosphocellulose chromatography and characterized with regard to several parameters which may regulate their activity in vivo . CK 1 has an NaCl optimum of 0.14 m , utilizes GTP as phosphate donor ~25% as efficiently as ATP, and phosphorylates a discrete group of high molecular weight nonhistone proteins in the unfractionated chromatin starting material. CK 2 has an NaCl optimum of 0.24 m , cannot utilize GTP, and modifies a different group of nonhistones. Both kinases are inhibited by concentrations of hemin (<50 μ m ) which efficiently induce globin gene expression in erythroleukemia cells. A histone kinase resolved during the gel filtration step is unaffected by hemin. An investigation of the mode of hemin inhibition reveals that CK 1 and CK 2 interact in different fashions with the inhibitor." @default.
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- W2067844128 title "Nucleosome-associated protein kinases in murine erythroleukemia cells" @default.
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- W2067844128 doi "https://doi.org/10.1016/0003-9861(79)90266-2" @default.
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