Interaction in vitro of scallop muscle arginine kinase with filamentous actin
| Autor: | S. Raghupathi Rami Reddy, C. Roustan, Ahmed Houmeida, Y. Benyamin |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Arginine
Fluorescence Polarization macromolecular substances Plasma protein binding Biochemistry Filamentous actin Adenosine Triphosphate Animals Actin chemistry.chemical_classification biology Muscles Arginine Kinase Arginine kinase Actins Enzyme assay In vitro Adenosine Diphosphate Kinetics Enzyme chemistry Mollusca biology.protein Rabbits Protein Binding |
| Zdroj: | European Journal of Biochemistry. 206:251-257 |
| ISSN: | 1432-1033 0014-2956 |
| DOI: | 10.1111/j.1432-1033.1992.tb16923.x |
| Popis: | Scallop muscle arginine kinase binds to F-actin from mollusc and rabbit muscle in vitro. One site of interaction appears to be located in residues 305-325 of a C-terminal fragment (residues 285-375) of actin. The binding is hindered in the presence of arginine, Mg(2+)-ADP and NO3-, which form a dead-end complex with the enzyme. F-actin inhibits the enzyme activity non-competitively with respect to Mg(2+)-ATP. As a function of arginine concentration, the inhibition is of the mixed type, where Km is affected more than Vmax. |
| Databáze: | OpenAIRE |
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