The Myotonin-Protein Kinase Phosphorylates Tyrosine Residues in Normal Human Skeletal Muscle
Copyright policy )The Myotonin-Protein Kinase Phosphorylates Tyrosine Residues in Normal Human Skeletal Muscle
As a first approach to study the cellular events involved in myotonic dystrophy, we have produced a polyclonal antibody against a peptide sequence of the predicted gene product. This antibody specifically recognizes a 54 kDa protein in human skeletal muscle. This protein phosphorylates a co-polymer Glu/Tyr but not Myelin Basic Protein. This indicates that the myotonin-protein kinase has a tyrosine kinase activity in human skeletal muscle. This is the first demonstration of the kinase activity of the myotonin-protein kinase.
Recombinant Fusion Proteins, Molecular Sequence Data, Muscle Proteins, Protein Serine-Threonine Kinases, Protein-Tyrosine Kinases, Myotonin-Protein Kinase, Immunologic Techniques, Humans, Myotonic Dystrophy, Tyrosine, Amino Acid Sequence, Cloning, Molecular, Peptides, Phosphotyrosine, Protein Kinases
Recombinant Fusion Proteins, Molecular Sequence Data, Muscle Proteins, Protein Serine-Threonine Kinases, Protein-Tyrosine Kinases, Myotonin-Protein Kinase, Immunologic Techniques, Humans, Myotonic Dystrophy, Tyrosine, Amino Acid Sequence, Cloning, Molecular, Peptides, Phosphotyrosine, Protein Kinases
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