A major lienal phosphotyrosine phosphatase is inhibited by phospholipids and inositol trisphosphate
| Autor: | Hans Werner Hofer, Christine Stader |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Phytic Acid
Swine T-Lymphocytes Phosphatase Biophysics Phospholipid Inositol 1 4 5-Trisphosphate Protein tyrosine phosphatase Biology Biochemistry Chromatography DEAE-Cellulose chemistry.chemical_compound Animals Humans Inositol phosphate Molecular Biology Phospholipids chemistry.chemical_classification Inositol trisphosphate Tyrosine phosphorylation Cell Biology Kinetics Enzyme chemistry Protein Tyrosine Phosphatases Tyrosine kinase Spleen Subcellular Fractions |
| Zdroj: | Biochemical and Biophysical Research Communications. 189:1404-1409 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(92)90230-i |
| Popis: | A major "non-receptor" phosphotyrosine-specific protein phosphatase isolated from the 30,000g pellet fraction of porcine spleen is related to the human T-cell tyrosine phosphatase (Cool et al. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 5257-5261) and is strongly inhibited by micromolar concentrations of phosphatidyl inositol (IC50 6 microM) and phosphatidyl serine (IC50 3.7 microM). In addition, the enzyme is inhibited by myo-inositol 1,4,5-trisphosphate (IC50 ca. 2 microM) in a non-competitive manner but not by myo-inositol hexaphosphate. Since the overall cellular tyrosine phosphatase activity greatly exceeds tyrosine kinase activity, inhibition of the phosphatase may be of importance for the regulation of the extent of tyrosine phosphorylation of cellular proteins. |
| Databáze: | OpenAIRE |
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