ISOLATION AND CHARACTERIZATION OF A 34000-DALTON CALMODULIN-BINDING AND F-ACTIN-BINDING PROTEIN FROM CHICKEN GIZZARD SMOOTH-MUSCLE
ISOLATION AND CHARACTERIZATION OF A 34000-DALTON CALMODULIN-BINDING AND F-ACTIN-BINDING PROTEIN FROM CHICKEN GIZZARD SMOOTH-MUSCLE
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DOI：
10.1016/s0006-291x(86)80328-x
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发表时间：
1986-11-26
影响因子：
3.1
通讯作者：
KOKUBU, T
中科院分区：
文献类型：
--
作者：
TAKAHASHI, K;HIWADA, K;KOKUBU, T
利用硫酸铵分级分离、阳离子交换层析和凝胶过滤的方法，从鸡平滑肌的热溶性组分中分离到一个分子量为34000-道尔顿的蛋白质。肌匀浆中34000-道尔顿蛋白的含量与原肌球蛋白相当。34000-道尔顿蛋白与F-actin和F-actin-tropomyosin的结合不依赖于Ca ~（2+），但与钙调素的结合依赖于Ca ~（2+）。我们暂时将34000-道尔顿蛋白质命名为砂囊p34 K。
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.