Yonago Acta medica 1998;41:31–44
Studies on a Ca2+- and Cyclic Nucleotide-Independent H1 Histone Kinase Purified from Rabbit Skeletal Muscle
Norika Kubota, Toshie Akagi, Kazuhiro Kueda, Sawako Saito, Eiji Nanba*, Barry
S. BrewsterÝ, Peter N. StrongÝ and Eikichi Hashimoto
Department of Pathological Biochemistry, Faculty of Medicine and *Gene Research
Center, Tottori University, Yonago 683-0826 Japan and ÝNeuromuscular Unit, Royal Postgraduate Medical School, Hammersmith Hospital, London W12 ONN United Kingdom
In an attempt to elucidate the regulatory mechanism of microsomal function
by protein phosphorylation, one of the major protein kinases obtained during the
preparation of the microsomal fraction of rabbit skeletal muscle was partially purified
and characterized. This enzyme was a protein serine/threonine kinase and showed similar,
but not completely same properties as those of Ca 2+-phospholipid-dependent
protein kinase (protein kinase C), judging from its elution profile from an anion-exchange
column, molecular mass, responses to protein kinase activators or inhibitors and
the substrate specificity. These results suggest a possible implication of this Ca 2+-
and cyclic nucleotide-independent H1 histone kinase in protein phosphorylation of
microsomal protein(s), although the exact role and the mechanism of regulation of
this enzyme are not clear at this time.
Key words: H1 histone kinase; microsome; protein kinase C; protein phosphorylation; skeletal muscle (rabbit)
