Flickinger C J, Herr J C, Ertl K E
J Androl. 1986 May-Jun;7(3):163-8. doi: 10.1002/j.1939-4640.1986.tb00903.x.
Proteins of mouse cauda epididymal fluid were analyzed by polyacrylamide gel electrophoresis. Fluid expressed from the cauda epididymidis and samples obtained by micropuncture of the epididymal lumen showed very similar patterns with respect to the major proteins they contained, with the exception of a small amount of serum albumin found in expressed caudal fluid. Eight prominent peptides present in both micropuncture fluid and expressed caudal epididymal fluid were selected for further study, and were designated CP 47, 42, 35, 29, 27, 25, 18, and 13 according to their mobility. Six of these were never detected in serum. Periodic acid-Schiff staining indicated that at least three were glycoproteins. The epididymal proteins were purified by preparative polyacrylamide gel electrophoresis and electroelution. Upon re-electrophoresis, the individual purified peptides comigrated with the corresponding bands in whole epididymal fluid, and no additional bands were detected, indicating that the proteins were purified to a high degree of homogeneity. Several of the mouse epididymal peptides resemble in their mobility proteins identified previously in other species, most notably the widely studied 33 Kd and 16 to 18 Kd proteins detected in the rat.
采用聚丙烯酰胺凝胶电泳对小鼠附睾尾部液体中的蛋白质进行了分析。从附睾尾部挤出的液体以及通过附睾管腔微穿刺获得的样本，就其所含的主要蛋白质而言，显示出非常相似的模式，但在挤出的尾部液体中发现了少量血清白蛋白。选择在微穿刺液和挤出的附睾尾部液体中均存在的8种显著肽段进行进一步研究，并根据其迁移率分别命名为CP 47、42、35、29、27、25、18和13。其中6种在血清中从未被检测到。过碘酸-希夫染色表明，其中至少3种是糖蛋白。通过制备性聚丙烯酰胺凝胶电泳和电洗脱对附睾蛋白质进行了纯化。重新电泳时，各个纯化的肽段与整个附睾液体中的相应条带共迁移，未检测到其他条带，这表明蛋白质已被纯化至高度均一。几种小鼠附睾肽段的迁移率与先前在其他物种中鉴定出的蛋白质相似，最显著的是在大鼠中广泛研究的33 Kd和16至18 Kd蛋白质。
