Adenylate deaminase binding to synthetic thick filaments of myosin.
AUTOR(ES)
Koretz, J F
RESUMO
Adenylate deaminase (AMP deaminase; AMP aminohydrolase, EC 3.5.4.6), a tetrameric enzyme found at particularly high concentrations in skeletal muscle, has previously been shown to bind strongly to the subfragment-2-portion of myosin in vitro and to the ends of the A band in vivo. It is shown here that when adenylate deaminase is dialyzed with skeletal myosin during formation of synthetic filaments at pH 7.0 it decorates the filament at 14.3-nm intervals, presumably in the region of exposed backbone between crossbridge levels. Optical diffraction of the aggregates reveals both enhancement of reflections arising from underlying myosin organization and other reflections arising from adenylate deaminase arrangement on the filament surface. Adenylate deaminase can thus be used as a specific label in the study of myosin presence and organization.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=350466Documentos Relacionados
- Dynamic exchange of myosin molecules between thick filaments.
- Myosin light chain phosphorylation affects the structure of rabbit skeletal muscle thick filaments.
- Structural studies of isolated native thick filaments from rabbit psoas muscle with AMP deaminase decoration.
- Yeast actin filaments display ATP-dependent sliding movement over surfaces coated with rabbit muscle myosin.
- Dynamic electron microscopy of ATP-induced myosin head movement in living muscle thick filaments
