Abstract
During purification of tau protein kinase I and II from the bovine brain extract, a new tau protein kinase was detected and purified with phosphocellulose, gel filtration, S-Sepharose and AF-Heparin column chromatography. The molecular mass of the enzyme was determined to be 32 kDa by gel filtration and activity staining on SDS-PAGE. The enzyme is a Ser/Thr protein kinase phosphorylating tau, beta-tubulin, MAP2 and alpha-casein. Employing many synthetic peptides, the recognition site of this enzyme appears to be -SR-. The enzyme requires no second messenger and is inhibited with high concentration of heparin, but not by inhibitors of CKI. These results indicate that this enzyme, tau-tubulin kinase is novel and distinct from TPKI, II and CKI, II.
MeSH terms
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Adenosine Triphosphate / metabolism
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Amino Acid Sequence
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Animals
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Brain / enzymology*
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Caseins / metabolism
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Cattle
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Chromatography
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Electrophoresis, Polyacrylamide Gel
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Heparin / pharmacology
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Histones / metabolism
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Kinetics
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Microtubule-Associated Proteins / metabolism
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Molecular Sequence Data
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Molecular Weight
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Peptides / chemistry
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Peptides / metabolism
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Phosphorylation
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Potassium Chloride / pharmacology
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Protein Serine-Threonine Kinases / chemistry
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Protein Serine-Threonine Kinases / isolation & purification*
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Protein Serine-Threonine Kinases / metabolism*
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Substrate Specificity
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Tubulin / metabolism*
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tau Proteins / metabolism*
Substances
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Caseins
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Histones
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Microtubule-Associated Proteins
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Peptides
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Tubulin
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tau Proteins
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Potassium Chloride
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Adenosine Triphosphate
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Heparin
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tau-tubulin kinase
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Protein Serine-Threonine Kinases