Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments

Tau protein kinase I (TPKI) isolated from bovine brain has been determined to phosphorylate tau at four distinct sites by detecting modified Ser and Thr residues with protein sequencer. Ser199, Thr231, Ser396 and Ser413 were all found to have been phosphorylated by TPKI (numbering of amino acids was...

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Veröffentlicht in:	Neuroscience letters 1992-12, Vol.148 (1), p.202-206
Hauptverfasser:	Ishiguro, Koichi, Omori, Akira, Takamatsu, Masako, Sato, Kazuki, Arioka, Manabu, Uchida, Tsuneko, Imahori, Kazutomo
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer disease Amino Acid Sequence Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Electrophoresis, Polyacrylamide Gel Epitopes - analysis Fundamental and applied biological sciences. Psychology Glycogen Synthase Kinase 3 Immunoblotting Isoenzymes - metabolism Kinetics Microtubule Microtubules - metabolism Miscellaneous Molecular Sequence Data Molecular Weight Paired helical filament Peptide Fragments - isolation & purification Phosphopeptides - isolation & purification Phosphorylation Protein kinase Protein Kinases - metabolism Protein-Serine-Threonine Kinases - metabolism Proteins Tau protein tau Proteins - immunology tau Proteins - isolation & purification tau Proteins - metabolism Tubulin - metabolism
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