| Autor: |
V P, Kirillina, V I, Stabrovskaya, Borovikov YuS |
| Rok vydání: |
1989 |
| Předmět: |
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| Zdroj: |
General physiology and biophysics. 8(5) |
| ISSN: |
0231-5882 |
| Popis: |
The changes in conformation of F-actin induced by the binding of the glycolytic enzyme lactate dehydrogenase were studied in myosin-free single ghost muscle fibres. The formation of the lactate dehydrogenase-F-actin complex was accompanied by changes in the parameters of intrinsic (tryptophan) and extrinsic (rhodaminyl-phalloin) polarized fluorescence of ghost muscle fibre F-actin. Lactate dehydrogenase stimulated actin-activated Mg2+-ATPase of myosin subfragment 1 by 30%. F-actin of ghost fibres depressed lactate dehydrogenase activity to 20% of the initial values. It is suggested that the energy-providing mechanism is coupled with that of muscle contraction through conformational changes in F-actin. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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