Isolation of alpha-actinin from sarcoma 180 ascites cells plasma membranes and comparison with smooth muscle alpha-actinin.
alpha-Actinin from Sarcoma 180 ascites cell plasma membranes was purified after extraction in 10 mM Tris, 1 mM EDTA, 1 mM mercaptoethanol, pH 8.5, by chromatography on DEAE and hydroxyapatite for comparisons with smooth muscles alpha-actinin purified from turkey gizzard by the same procedure. The two proteins were found to be very similar by sedimentation analysis, gel filtration and dodecyl sulfate gel electrophoresis. Direct comparisons of smooth muscle, skeletal muscle and ascites alpha-actinin by amino acid analysis indicated a closer relationship between the smooth muscle and ascites proteins than between the smooth and skeletal muscle proteins. Both smooth muscle and ascites alpha-actinins cross-link F-actin filaments. The results suggest that the smooth muscle protein is a better system for understanding properties of non-muscle alpha-actinins than is the skeletal muscle protein.
D000185:Actinin / Q000302:isolation & purification* / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000818:Animals; D001201:Ascites / Q000378:metabolism*; D002462:Cell Membrane / Q000032:analysis; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D009124:Muscle Proteins / Q000302:isolation & purification*; D009130:Muscle, Smooth / Q000032:analysis*; D012510:Sarcoma 180 / Q000032:analysis*; D014422:Turkeys
D000199:Actins; D009124:Muscle Proteins; D000185:Actinin