Calcium- and calmodulin-dependent phosphorylase kinase activity in porcine uterine smooth muscle
| Autor: | Eikichi Hashimoto, Keiko Mizuta, Hirohei Yamamura, Akimitsu Tsutou, Akira Negami, Shun-ichi Nakamura |
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| Rok vydání: | 1985 |
| Předmět: |
medicine.medical_specialty
Calmodulin Phosphorylase Kinase Swine Biophysics chemistry.chemical_element Stimulation Trifluoperazine Calcium Biochemistry chemistry.chemical_compound Internal medicine medicine Animals Phosphorylase kinase Molecular Biology chemistry.chemical_classification biology Uterus Myometrium Cell Biology Hydrogen-Ion Concentration Cell biology Enzyme Activation EGTA Kinetics Enzyme Endocrinology chemistry biology.protein Female medicine.drug |
| Zdroj: | Biochemical and biophysical research communications. 126(1) |
| ISSN: | 0006-291X |
| Popis: | Porcine uterine smooth muscle phosphorylase kinase has been partially purified. The enzyme was activated about 1.5–2.0-fold by exogenous calmodulin. Half maximal stimulation was observed at about 100 nM calmodulin. The activation was dependent on calcium and was maximum at pH 7.5 in the range of pH from 6 to 9. This activation was completely abolished by 100 μM trifluoperazine. The result suggested that unlike slow and cardiac muscles, phosphorylase kinase of uterine smooth muscle showed similar response to calmodulin with that of fast muscle. The physiological role of the calcium and calmodulin-dependent activation of myometrium phosphorylase kinase is briefly discussed. |
| Databáze: | OpenAIRE |
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