P. Etonguemayer et al., THE MYOTONIN-PROTEIN KINASE PHOSPHORYLATES TYROSINE RESIDUES IN NORMAL HUMAN SKELETAL-MUSCLE, Biochemical and biophysical research communications, 199(1), 1994, pp. 89-92
As a first approach to study the cellular events involved in myotonic
dystrophy, we have produced a polyclonal antibody against a peptide se
quence of the predicted gene product. This antibody specifically recog
nizes a 54 kDa protein in human skeletal muscle. This protein phosphor
ylates a co-polymer Glu/Tyr but not Myelin Basic Protein. This indicat
es that the myotonin-protein kinase has a tyrosine kinase activity in
human skeletal muscle. This is the first demonstration of the kinase a
ctivity of the myotonin-protein kinase. (C) 1994 Academic Press, Inc.