Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreas
| Autor: | Angus C. Nairn, M J Brady, H C Palfrey, Ken-ichi Mitsui |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
chemistry.chemical_classification
Gel electrophoresis education.field_of_study Cell Biology Biology Mitogen-activated protein kinase kinase Biochemistry Molecular biology MAP2K7 Enzyme chemistry Ca2+/calmodulin-dependent protein kinase Phosphorylation Elongation Factor-2 Kinase education Protein kinase A Molecular Biology |
| Zdroj: | Journal of Biological Chemistry. 268:13422-13433 |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/s0021-9258(19)38667-3 |
| Popis: | Calmodulin-dependent protein kinase III (CaM kinase III) phosphorylates and thereby inactivates eukaryotic elongation factor-2 (EF-2). This enzyme, purified to homogeneity from either rabbit reticulocytes or rat pancreas, had similar properties: it migrated with an apparent M(r) of 140,000 by gel filtration, was comprised of a major polypeptide of M(r) 95,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and had a high affinity for CaM (half-maximal activation |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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