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Tytuł oryginału: The effects of the interaction of myosin essential light chain isoforms with actin in skeletal muscles.
Autorzy: Nieznańska Hanna, Nieznański Krzysztof, Stępkowski Dariusz
Źródło: Acta Bioch. Pol. 2002: 49 (3) s.709-719, il., tab., bibliogr. 717-719
Sygnatura GBL: 303,116

Typ dokumentu:
  • praca doświadczalna
  • tytuł obcojęzyczny

    Wskaźnik treści:
  • zwierzęta
  • króliki

    Streszczenie angielskie: In order to compare the ability of different isoforms of myosin essential light chain to interact with actin, the effect of the latter protein on the proteolytic susceptibility of myosin light chains (MLC-1S and MLC-1V - slow specific and same as ventricular isoform) from slow skeletal muscle was examined. Actin protects both slow muscle essential light chain isoforms from papain digestion, similarly as observed for fast skeletal muscle myosin (Nieznańska et al., 1998, Biochim. Biophys. Acta 1383: 71). The effect of actin decreases as ionic strength rises above physiological values for both fast and slow skeletal myosin, confirming the ionic character of the actin - essential light chain interaction. To better understand the role of this interaction, we examined the effect of synthetic peptide spanning the 10-amino-acid n-terminal sequences of myosin light chain 1 from fast skeletal muscle (MLC-1F0 (MLCFpep: KKDVKKPAAA), MLC-1S (MLCSpep: KKDVPVKKPA) and MLC-1V (MLCVpep: KPEPKKDDAK) on the myorfibrillar ATPase of fast and slow skeletal muscle. In the presence of MLCFpep, we observed an about 19 p.c. increase, and in the presence of MLCSpepabout 36 p.c. increase, in the myofibrillar ATPase activity of fast muscle. On the other hand, in myofibrillar preparations from slow skeletal muscle, MLCSpep as well as MLCVpep caused a lowering of the ATPase activity by about 36 p.c. The above results suggest that MLCSpep induces opposite effects on ATPase activity, depending on the type of myofibrils, but not through its specific N-terminal sequence - which differs from other MLC N-terminal peptides...

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