Hosoya H, Iwasa F, Ohnuma M, Mabuchi I, Mohri H, Sakai H, Hiramoto Y
FEBS Lett. 1986 Sep 1;205(1):121-6. doi: 10.1016/0014-5793(86)80878-x.
A novel Ca2+-binding protein, different from calmodulin, has been purified to homogeneity from the soluble cytoplasmic protein fraction of the egg of the sea urchin, Hemicentrotus pulcherrimus. This protein, designated as 15 kDa protein, shows a Ca2+-dependent mobility shift upon SDS-gel electrophoresis and has Ca2+-binding ability. This protein did not resemble the sea urchin egg calmodulin in either molecular mass or amino acid composition. The 15 kDa protein could not activate cyclic adenosine 3',5'-monophosphate-dependent phosphodiesterase from bovine brain and did not bind to fluphenazine-Sepharose 6B. Antibodies against the 15 kDa protein did not react with sea urchin egg calmodulin. These results suggest that the 15 kDa protein is a novel Ca2+-binding protein in the sea urchin egg.
一种不同于钙调蛋白的新型钙离子结合蛋白已从海胆(Hemicentrotus pulcherrimus)卵的可溶性细胞质蛋白组分中纯化至同质。这种被命名为15 kDa蛋白的蛋白质在SDS凝胶电泳时表现出钙离子依赖性的迁移率变化,并且具有钙离子结合能力。该蛋白质在分子量或氨基酸组成上均与海胆卵钙调蛋白不同。15 kDa蛋白不能激活来自牛脑的环磷酸腺苷依赖性磷酸二酯酶,也不与氟奋乃静 - 琼脂糖6B结合。针对15 kDa蛋白的抗体不与海胆卵钙调蛋白发生反应。这些结果表明,15 kDa蛋白是海胆卵中的一种新型钙离子结合蛋白。