Cargando…
Isolation and partial characterization of a 110-kD dimer actin-binding protein
Two Triton-insoluble fractions were isolated from Acanthamoeba castellanii. The major non-membrane proteins in both fractions were actin (30-40%), myosin II (4-9%), myosin I (1-5%), and a 55-kD polypeptide (10%). The 55-kD polypeptide did not react with antibodies against tubulins from turkey brain,...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1986
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2113839/ https://www.ncbi.nlm.nih.gov/pubmed/2942552 |
Ejemplares similares
-
The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase
Publicado: (1987) -
Mapping of the microvillar 110K-calmodulin complex: calmodulin- associated or -free fragments of the 110-kD polypeptide bind F-actin and retain ATPase activity
Publicado: (1988) -
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) -
Preparation and Characterization of a Polyclonal Antibody against Human Actin Filament-Associated Protein-120 kD
por: Chen, Yujian, et al.
Publicado: (2016) -
Comparative characterization of the 21-kD and 26-kD gap junction proteins in murine liver and cultured hepatocytes
Publicado: (1989)