Gimona M, Fürst D O, Small J V
Institute of Molecular Biology, Austrian Academy of Sciences, Salzburg.
J Muscle Res Cell Motil. 1987 Aug;8(4):329-41. doi: 10.1007/BF01568889.
Metavinculin, a vinculin related protein found only in muscle, has been prepared in bulk amounts from porcine stomach by a new procedure: the same procedure is applicable to the purification of vinculin from porcine stomach and avian gizzard. A comparison of the mammalian and avian proteins by peptide mapping showed them all to contain a common protease resistant 90 kDa core; however both avian and mammalian vinculins were notably more resistant to proteolysis down to this core than their respective metavinculins. Despite the close similarities in the peptide maps, in molecular weight and amino acid composition neither of the mammalian proteins exhibited the head and tail morphology formerly described for gizzard vinculin and metavinculin; both porcine proteins appeared globular under the electron microscope. From the gross variability in the ratios of metavinculin to vinculin among smooth muscles of different origin as well as from the common detergent-independent solubility properties of both proteins during isolation, it is concluded that vinculin and metavinculin perform duplicatory roles as peripheral membrane components. No definitive evidence for the interaction of either protein with actin filaments was obtained.
变旋联蛋白是一种仅在肌肉中发现的与纽蛋白相关的蛋白质，已通过一种新方法从猪胃中大量制备出来：该方法同样适用于从猪胃和禽肌胃中纯化纽蛋白。通过肽图谱对哺乳动物和禽类蛋白质进行比较，结果显示它们均含有一个共同的抗蛋白酶90 kDa核心；然而，禽类和哺乳动物的纽蛋白在降解至该核心时，比各自的变旋联蛋白对蛋白水解的抗性明显更强。尽管肽图谱、分子量和氨基酸组成非常相似，但两种哺乳动物蛋白质均未呈现出先前描述的肌胃纽蛋白和变旋联蛋白的头尾形态；在电子显微镜下，两种猪蛋白均呈球状。鉴于不同来源平滑肌中变旋联蛋白与纽蛋白比例的巨大差异，以及两种蛋白质在分离过程中共同的不依赖去污剂的溶解性，得出结论：纽蛋白和变旋联蛋白作为外周膜成分发挥重复作用。未获得任何一种蛋白质与肌动蛋白丝相互作用的确切证据。
