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• W2045279209 abstract "Abstract A kinase phosphorylating casein and phosvitin has been purified from pine pollen by a three-step procedure involving DEAE-cellulose chromatography, affinity chromatography on casein-Sepharose and Sephadex G-100. A purification of about 2000 fold was obtained by this procedure. The kinase is affected neither by cyclic nucleotides nor by Ca 2+ -calmodulin, whereas it is strongly inhibited by heparin. Using this purification procedure, we have isolated protein kinase exhibiting phosphorylating activity towards casein in the pollen of many other Pinaceae species." @default.
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• W2045279209 date "1984-01-01" @default.
• W2045279209 modified "2023-10-17" @default.
• W2045279209 title "Purification and characterization of a protein kinase from pine pollen" @default.
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• W2045279209 doi "https://doi.org/10.1016/0031-9422(84)83005-8" @default.
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