Garberi J C, Kohane A C, Cameo M S, Blaquier J A
Mol Cell Endocrinol. 1979 Jan;13(1):73-82. doi: 10.1016/0303-7207(79)90077-7.
The partial purification and characterization of specific rat epididymal proteins (SEP) is reported. Starting from the cytosol fraction obtained from epididymal homogenates, protein C was purified 15-fold and proteins D--E were purified 19-fold. The molecular weight, determined by molecular sieving, of protein C was 22,400 while that of D--E was 37,000. These proteins stained as glycoproteins with periodic acid--Schiff reagent. The isoelectric point of protein D was 5.13 while that of protein E was 4.95. Protein C separated into 3 bands during isoelectric focussing. The major component focussed at 5.56 and the two minor components at pH 5.38 And 5.79. Using a specific antiserum we could confirm the organ specificity of SEP and their androgen-dependence.
本文报道了大鼠附睾特异性蛋白（SEP）的部分纯化及特性研究。从附睾匀浆获得的胞质部分开始，蛋白C纯化了15倍，蛋白D - E纯化了19倍。通过分子筛测定，蛋白C的分子量为22,400，而蛋白D - E的分子量为37,000。这些蛋白用高碘酸 - 希夫试剂染色呈糖蛋白。蛋白D的等电点为5.13，蛋白E的等电点为4.95。蛋白C在等电聚焦过程中分离成3条带。主要成分聚焦在5.56，两个次要成分分别在pH 5.38和5.79。使用特异性抗血清，我们可以证实SEP的器官特异性及其雄激素依赖性。
