Simplified co-purification of vascular smooth muscle calponin and caldesmon.
A method for the co-purification of calponin and caldesmon from bovine aorta smooth muscle was established involving heat treatment, ammonium sulfate fractionation (0-30 and 30-50%), CM52 column chromatography, and Ultrogel AcA44 gel filtration. The yields of calponin and caldesmon from 200 g of smooth muscle were 17 and 32 mg, respectively. This simplified, fast, and efficient method for the purification of calponin and caldesmon constitutes a useful tool for studying thin filament-linked regulation of smooth muscle contraction.
Abe
M
M
Second Department of Internal Medicine, Ehime University School of Medicine.
Takahashi
K
K
Hiwada
K
K
D000818:Animals; D001011:Aorta / Q000032:analysis; D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D002148:Calmodulin-Binding Proteins / Q000302:isolation & purification*; D002417:Cattle; D004591:Electrophoresis, Polyacrylamide Gel; D008840:Microfilament Proteins; D009131:Muscle, Smooth, Vascular / Q000032:analysis*; D000096985:Calponins
D002135:Calcium-Binding Proteins; D002148:Calmodulin-Binding Proteins; D008840:Microfilament Proteins; D000096985:Calponins