肌肉肌动蛋白丝在体外可结合垂体分泌颗粒。
Muscle actin filaments bind pituitary secretory granules in vitro.
作者信息
Ostlund R E, Leung J T, Kipnis D M
出版信息
J Cell Biol. 1977 Apr;73(1):78-87. doi: 10.1083/jcb.73.1.78.
Abstract
Hog anterior pituitary secretory granules sediment at 3,000 g. When rat or rabbit skeletal muscle actin filaments are present with the granules, the sedimentation decreases markedly. Depolymerized actin or viscous solutions of Ficoll and collagen have no effect on granule sedimentation. With this assay, actin filaments bind secretory granules (consisting of the proteinaceous core plus limiting membrane), secretory granule membranes, mitochondria, artificial lecithin liposomes, and styrene-butadiene microspheres, but have little or no interaction with membrane-free secretory granule cores and albumin microspheres. A secretory granule-actin complex sedimentable between 3,000 g and 25,000 g can be isolated. Metal ions, nucleotides, salts, dithiothreitol, or pretreatment of the granules with trypsin do not destroy the binding, which appears to be a lipophilic interaction.
摘要
猪垂体前叶分泌颗粒在3000g的离心力下会发生沉降。当大鼠或兔骨骼肌肌动蛋白丝与这些颗粒同时存在时，沉降会显著减少。解聚的肌动蛋白或菲可和胶原蛋白的粘性溶液对颗粒沉降没有影响。通过这种测定方法，肌动蛋白丝能结合分泌颗粒（由蛋白质核心加上限制膜组成）、分泌颗粒膜、线粒体、人工卵磷脂脂质体和丁苯橡胶微球，但与无膜的分泌颗粒核心和白蛋白微球几乎没有相互作用。可以分离出一种在3000g至25000g之间可沉降的分泌颗粒 - 肌动蛋白复合物。金属离子、核苷酸、盐、二硫苏糖醇或用胰蛋白酶对颗粒进行预处理不会破坏这种结合，这种结合似乎是一种亲脂性相互作用。
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