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The influence of body temperature and castration on the protein composition of fluid in the rat cauda epididymidis

Summary. Polyacrylamide gel electrophoresis under reducing and non-reducing conditions, and immunoelectrophoretic analysis, revealed that several characteristic proteins disappear from the luminal fluid of the rat cauda epididymidis when it is maintained at body temperature. On SDS-PAGE gels prepared under reducing conditions, one Coomassie-blue staining band of M_r 18 000 disappeared and another of 52 000 was significantly reduced after only 6 days; bands of M_r 23 000, several in the M_r 34–38 000 range, one of M_r 48 000, and others of M_r 100–200 000 were eliminated or markedly reduced after 15 days at body temperature. Some were glycoprotein, as judged by their affinity for FITC–ConA. At 15 days after castration there was a broadly similar but rather more extensive disappearance of macromolecules, and of glycoproteins in particular, from caudal fluid. The fact that several similar proteins are diminished in or disappear from fluid or the cauda epididymidis maintained at body temperature, or after androgen withdrawal, raises the possibility that one or more such proteins play a role in sperm storage there.

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				M. Jara, P. Esponda, and R. Carballada Abdominal Temperature Induces Region-Specific p53-Independent Apoptosis in the Cauda Epididymidis of the Mouse Biol Reprod, October 1, 2002; 67(4): 1189 - 1196. [Abstract] [Full Text] [PDF]