Role of the C-terminal extremities of the smooth muscle myosin heavy chains: implication for assembly properties
| Autor: | Georges Foucault, Anne-Marie Lompré, Sophie Quevillon-Cheruel, Michel Desmadril, Jean-Jacques Bechet |
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| Rok vydání: | 1999 |
| Předmět: |
Gene isoform
Myosin light-chain kinase Protein Conformation Assembly Molecular Sequence Data Biophysics macromolecular substances Biochemistry law.invention Contractility Myosin head Smooth muscle Structural Biology law Myosin Genetics Escherichia coli Animals Molecular Biology Meromyosin Heavy meromyosin Base Sequence Myosin Heavy Chains Chemistry Muscle Smooth Cell Biology Hydrogen-Ion Concentration Recombinant Proteins Solubility Recombinant DNA Rabbits Myosin heavy chain |
| Zdroj: | FEBS letters. 454(3) |
| ISSN: | 0014-5793 |
| Popis: | The two light meromyosin isoforms from rabbit smooth muscle were prepared as recombinant proteins in Escherichia coli. These species which differed only by their C-terminal extremity showed the same circular dichroism spectra and endotherms in measurements of differential scanning calorimetry. Their solubility properties were different at pH 7.0 in the absence of monovalent salts. Their paracrystals formed at low pH differed by their aspect and number. These data suggest a role for the C-terminal extremity of myosin heavy chains in the assembly of myosin molecules in filaments and consequently in the contractility of smooth muscles. |
| Databáze: | OpenAIRE |
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