Takahashi K, Hiwada K, Kokubu T
Biochem Biophys Res Commun. 1986 Nov 26;141(1):20-6. doi: 10.1016/s0006-291x(86)80328-x.
We isolated a 34,000-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 34,000-dalton protein in the muscle homogenate was as much as tropomyosin. The 34,000-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 34,000-dalton protein gizzard p34K.
我们使用硫酸铵分级分离、阳离子交换色谱和凝胶过滤的方法，从禽平滑肌的热可溶性部分中分离出一种34,000道尔顿的蛋白质。肌肉匀浆中34,000道尔顿蛋白质的含量与原肌球蛋白一样多。这种34,000道尔顿的蛋白质以不依赖Ca2+的方式与F-肌动蛋白和F-肌动蛋白-原肌球蛋白结合，但它与钙调蛋白以Ca2+依赖的方式相互作用。我们暂定将这种34,000道尔顿的蛋白质命名为砂囊p34K。
