Histone H1 kinase from mouse plasmacytoma. Further characterization and molecular structure

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Abstract
A cAMP-independent protein kinase which phosphorylates histone H1 to a high level and which may correspond to the mitotic H1 kinase was partially purified and characterized from mouse plasmacytoma microsomes (Quirin-Stricker, C., and Schmitt, M., 1981). The microsome-associated and the chromatin-associated histone H1 kinases isolated from mouse plasmacytoma cells were compared. The 2 H1 kinases are indistinguishable by several criteria. The molecular structure of the microsome-associated histone H1 kinase was determined by exclusion chromatography on Ultrogel; by electrophoresis in non-denaturing polyacrylamide gels of graded porosity; and by sodium dodecyl sulfate/polyacrylamide gel electrophoresis of the H1 kinase activity peak from an AcA-34 Ultrogel column. All these techniques gave the same result: H1 kinase may exist in a native form as a monomeric enzyme with an apparent relative molecular mass of 90,000 .+-. 8000.