Cargando…
Characterization of intestinal microvillar membrane disks: detergent- resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin)
The actin bundle within each microvillus of the intestinal brush border (BB) is tethered laterally to the membrane by bridges composed of BB myosin I. Avian BB myosin I, formerly termed 110K-calmodulin, consists of a heavy chain with an apparent Mr of 110 kD and three to four molecules of calmodulin...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1989
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115773/ https://www.ncbi.nlm.nih.gov/pubmed/2527857 |
Ejemplares similares
-
Nucleated polymerization of actin from the membrane-associated ends of microvillar filaments in the intestinal brush border
Publicado: (1982) -
Structural and immunological characterization of the myosin-like 110-kD subunit of the intestinal microvillar 110K-calmodulin complex: evidence for discrete myosin head and calmodulin-binding domains
Publicado: (1988) -
The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme
Publicado: (1989) -
Calmodulin dissociation regulates brush border myosin I (110-kD- calmodulin) mechanochemical activity in vitro
Publicado: (1990) -
Brush border motility. Microvillar contraction in triton-treated brush borders isolated from intestinal epithelium
Publicado: (1976)