Zobrazeno 1 - 10
of 109
pro vyhledávání: '"T. S. Ingebritsen"'
Autor:
Bhanu P. Jena, S. Jakes, T. S. Ingebritsen, J. Richards, Louisa B. Tabatabai, Bonnie L. Beck, K. L. Hippen
Publikováno v:
Biochemistry. 32:12405-12412
The mechanisms for substrate recognition by two cytoplasmic protein tyrosine phosphatases, PTP-5 and rrbPTP-1, were investigated. Phosphorylation sites on tyrosine-phosphorylated casein, a model PTP substrate, were characterized. Two peptides based o
Publikováno v:
Journal of Biological Chemistry. 266:10043-10046
pp54 microtubule-associated protein-2 (MAP-2) kinase, a recently discovered protein serine/threonine kinase (Kyriakis, J., and Avruch, J. (1990) J. Biol. Chem. 265, 17355-17363), is shown to contain immunoreactive phosphotyrosine residues. Treatment
Publikováno v:
Journal of Biological Chemistry. 266:17744-17746
Eukaryotic cells respond to various stimuli by an increase or decrease in levels of phosphoproteins. Phosphotyrosine levels on eukaryotic cellular proteins are tightly regulated by the opposing actions of protein-tyrosine kinases and protein-tyrosine
Autor:
John H. Connor, Lifang Zhang, Shogo Endo, Ernest Y.C. Lee, B. Forney, S. Shenolikar, T. S. Ingebritsen
Publikováno v:
Biochemistry. 36(23)
The phosphorylase phosphatase activity of protein phosphatase 1 (PP1) catalytic subunit from freshly purified rabbit skeletal muscle was inhibited by MnCl2. Prolonged storage or inhibition by nonspecific phosphatase inhibitors ATP, sodium pyrophospha
Publikováno v:
Analytical biochemistry. 223(1)
Thiophosphotyrosyl protein and peptide substrate analogs were found to be potent and specific protein-tyrosine phosphatase inhibitors with IC50s in the range of 0.2-30 microM. The analogs were based on highly reactive substrates and included thiophos
Publikováno v:
The Journal of biological chemistry. 266(16)
pp54 microtubule-associated protein-2 (MAP-2) kinase, a recently discovered protein serine/threonine kinase (Kyriakis, J., and Avruch, J. (1990) J. Biol. Chem. 265, 17355-17363), is shown to contain immunoreactive phosphotyrosine residues. Treatment
Autor:
T S, Ingebritsen
Publikováno v:
Methods in enzymology. 201
Publikováno v:
Biochemistry. 27:3216-3222
DNA topoisomerase I has been purified to electrophoretic homogeneity from ovaries of the frog Xenopus laevis. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the most purified fraction revealed a single major band at 110 kDa and less abu
Autor:
T S Ingebritsen
Publikováno v:
Journal of Biological Chemistry. 264:7754-7759
Two Tyr-protein phosphatase inhibitors, termed inhibitor H (Mr greater than 500,000) and inhibitor L (Mr 38,000), have been detected in bovine brain extracts. The inhibitors were partially purified by chromatography on DEAE-cellulose and Sephacryl S-
Publikováno v:
Biochemistry. 28:415-419
Rod cell outer segments were found to contain a protein phosphatase activity toward phosphoopsin with properties very similar to those of protein phosphatase 1 or 2A. The opsin phosphatase activity was stable to ethanol precipitation, had a Mr of 35,