Jones R, Hall L
Institute of Animal Physiology and Genetics Research, Cambridge Research Station, Babraham, U.K.
Biochim Biophys Acta. 1991 Oct 11;1080(1):78-82. doi: 10.1016/0167-4838(91)90114-f.
A 23 kDa protein that is a major component of rat epididymal secretions and sperm plasma membranes has been purified and partially sequenced. A data-base search revealed approximately 85% sequence similarity with a phosphatidyl-ethanolamine-binding protein from bovine brain cytosol. The rat 23 kDa protein also showed selective affinity for phosphatidylethanolamine (Kd = 1.6 x 10(-5) M) with lower activity towards phosphatidylinositol and phosphatidylcholine. It is suggested that differential affinity of protein antigens towards asymmetrically aligned phospholipids in sperm plasma membranes could account for their organisation into specific regional domains.
一种23千道尔顿的蛋白质已被纯化并进行了部分测序,它是大鼠附睾分泌物和精子质膜的主要成分。数据库搜索显示,它与来自牛脑细胞质的磷脂酰乙醇胺结合蛋白的序列相似度约为85%。大鼠的23千道尔顿蛋白质对磷脂酰乙醇胺也表现出选择性亲和力(解离常数Kd = 1.6×10⁻⁵ M),对磷脂酰肌醇和磷脂酰胆碱的活性较低。有人提出,蛋白质抗原对精子质膜中不对称排列的磷脂的不同亲和力可能解释了它们如何组织成特定的区域结构域。