Isolation and characterization of a 34000-dalton calmodulin-and F-actin-binding protein from chicken gizzard smooth muscle
K Takahashi, K Hiwada, T Kokubu - Biochemical and biophysical research …, 1986 - Elsevier
K Takahashi, K Hiwada, T Kokubu
Biochemical and biophysical research communications, 1986•ElsevierWe isolated a 34000-dalton protein from the heat-soluble fraction of avian smooth muscle
using the procedures of ammonium sulfate fractionation, cation exchange chromatography
and gel filtration. The amount of 34000-dalton protein in the muscle homogenate was as
much as tropomyosin. The 34000-dalton protein bound to F-actin and F-actin-tropomyosin in
a Ca 2+-independent manner, but it Ca 2+-dependently interacted with calmodulin. We
tentatively named the 34000-dalton protein gizzard p34K.
using the procedures of ammonium sulfate fractionation, cation exchange chromatography
and gel filtration. The amount of 34000-dalton protein in the muscle homogenate was as
much as tropomyosin. The 34000-dalton protein bound to F-actin and F-actin-tropomyosin in
a Ca 2+-independent manner, but it Ca 2+-dependently interacted with calmodulin. We
tentatively named the 34000-dalton protein gizzard p34K.
We isolated a 34000-dalton protein from the heat-soluble fraction of avian smooth muscle using the procedures of ammonium sulfate fractionation, cation exchange chromatography and gel filtration. The amount of 34000-dalton protein in the muscle homogenate was as much as tropomyosin. The 34000-dalton protein bound to F-actin and F-actin-tropomyosin in a Ca2+-independent manner, but it Ca2+-dependently interacted with calmodulin. We tentatively named the 34000-dalton protein gizzard p34K.
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