Creatine kinase binds more firmly to the M-band of rabbit skeletal muscle myofibrils in the presence of its substrates
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
- MeSH
- adenosintrifosfát metabolismus MeSH
- biologické modely MeSH
- fluorescenční barviva chemie MeSH
- fotovybělování MeSH
- konektin MeSH
- kosterní svalová vlákna metabolismus MeSH
- kosterní svaly metabolismus MeSH
- králíci MeSH
- kreatinkinasa, forma MM metabolismus MeSH
- svalové proteiny metabolismus MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- králíci MeSH
- mužské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- adenosintrifosfát MeSH
- fluorescenční barviva MeSH
- konektin MeSH
- kreatinkinasa, forma MM MeSH
- svalové proteiny MeSH
Creatine kinase (CK) (E.C. 2.7.3.2) buffers cellular ATP concentration during fluctuating ATP turnover. Muscle cytosolic CK isoform interacts with various subcellular structures where it is functionally coupled with relevant ATPases. However, how this interaction affects its activity is not known. We have therefore studied the interaction of CK with myofibrils and the role of different conformational states of CK molecule induced by ATP, phosphocreatine, ADP and the ATP-creatine pair. Purified rabbit psoas myofibrils with CK specific activity of 0.4+/-0.02 IU/mg were used. The exchange rates between the myofibrillar M-band and its surroundings were measured with fluorofore conjugated CK (IAF) by the Fluorescence Lost in Photobleaching (FLIP) method within a very narrow pH range 7.1-7.15. For CK-IAF without docked substrates, the time derivative of the initial loss of the fluorescent signal within the M-band equalled -3.26 at the fifth second and the decrease reached 82% by the 67th second. For CK-IAF with added substrates, the derivatives fell into the range of -0.95 to -1.30, with respective decreases from 16 to 46% at the 67th second. The results show that the substrates slowed down the exchange rate. This indicates that the strength of the bond between CK and the M-band of myofibrils increased.
Department of Physiology Faculty of Science Charles University Prague Prague 2 128 00 Czech Republic
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