Identification and androgen-dependence of proteins in the mouse vas deferens

Proteins from 'luminal fluid' or from a homogenate of whole vas deferens were analysed by polyacrylamide gel electrophoresis under denaturing conditions. Four major bands with apparent molecular weights of 34.5, 36, 38 and 180 Kilodaltons (K) were observed in homogenates. In 'luminal fluid' the same protein pattern was observed except that 38 K band was missing. These four major bands probably originated from the vas deferens as they were not detected in plasma and were still present after ligation between the epididymis and vas deferens. After castration, there was a specific reduction of the 34.5 K MW protein band in both homogenate and 'luminal fluid'. When the androgen-dependence of proteins was investigated using radioactive methionine, the protein spectra from normal and castrated males showed that about 10 polypeptides were differentially induced or repressed by androgens. The synthesis of some proteins (MW's 24, 36 and 180 K) was decreased by castration while the synthesis of several others (MW's between 27 and 82 K) was increased. Most of these androgen-dependent proteins were detectable at 10 days of age.