Open AccessHistone H1 kinase from mouse plasmacytoma
Author(s) -
QUIRINSTRICKER Christiane
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08288.x
Subject(s) - histone h1 , kinase , gel electrophoresis , microbiology and biotechnology , histone , chemistry , polyacrylamide gel electrophoresis , biochemistry , chromatin , biology , enzyme , dna
A cAMP‐independent protein kinase which phosphorylates histone H1 to a high level and which may correspond to the mitotic H1 kinase has been partially purified and characterized from mouse plasmacytoma microsomes [Quirin‐Stricker, C., and Schmitt, M. (1981) Eur. J. Biochem. 118 , 165–172]. The present study compares the microsome‐associated and the chromatin‐associated histone H1 kinases isolated from mouse plasmacytoma cells. The results indicate that the two H1 kinases are indistinguishable by several criteria. The molecular structure of the microsome‐associated histone H1 kinase has been determined (a) by exclusion chromatography on Ultrogel, (b) by electrophoresis in non‐denaturing polyacrylamide gels of graded porosity and (c) 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 90000 ± 8000.