PMID: 109328Jan 1, 1979

Isolation and characterization of specific rat epididymal proteins

Molecular and Cellular Endocrinology
J C GarberiJ A Blaquier


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.


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