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L. D. S. BARKER and R. P. AMANN

Summary.

Sites of protein absorption and secretion in the epididymis and changes in sperm antigenicity during their maturation and senescence were investigated. Tissue and sperm samples from normal bulls, unilaterally vasoligated bulls and bulls in which one epididymis was ligated distal to the caput epididymidis were examined using fluoresceinconjugated immune globulins. The globulins were obtained from antisera against spermatozoa from bull cauda epididymidis, ejaculated spermatozoa, plasma from the cauda epididymidis and seminal plasma. In mature spermatids, acrosomal immunofluorescence was homogeneous. After spermatozoa had traversed the first half of the caput epididymidis, the apical body was especially prominent. Specific immunofluorescence of the post-nuclear cap, cytoplasmic droplet, midpiece, and principal piece was not observed except in presumably senescent spermatozoa from spermatocoeles.

Non-ciliated, antigen-secreting cells were detected by their immunofluorescence in the epithelium of the efferent ducts within the proximal caput epididymidis. These secretory cells produce sperm-coating proteins which are antigenically similar to certain components of seminal vesicle fluid. Immunofluorescence of the apical cytoplasm and stereocilia in the proximal caput epididymidis indicated that this epithelium probably absorbed sperm-specific proteins emanating from the testis.

Immunofluorescence in the apical cytoplasm of the epithelium lining the corpus and proximal cauda epididymidis was suggestive of secretory activity. Similar fluorescence in the epithelium of the vas deferens may have resulted from the absorption of proteins.

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L. D. S. BARKER and R. P. AMANN

Summary.

Immunodiffusion and immunoelectrophoretic analyses, including absorption tests, were used to determine the heterogeneity of antigens in bull spermatozoa and reproductive fluids and to characterize antisera against these antigens. Antisera were produced against bull seminal plasma, seminal vesicle fluid, cauda epididymal plasma, blood serum, washed ejaculated spermatozoa, washed cauda epididymal spermatozoa and sperm fractions. Four sperm-specific antigens were detected. One antigen was located in the sperm head, one in the sperm tail and two others were common to both the head and tail. The tailspecific antigen was detected only after mechanical rupture of washed spermatozoa. The major antigens of spermatozoa are localized in the cell membrane and acrosome. Apparently, sperm antigens were present in cauda epididymal plasma and seminal plasma. These antigens may have been released by physiologically normal spermatozoa or they may represent end products of sperm dissolution within the epididymis and vas deferens. Their presence makes immunological analyses of reproductive fluids difficult.

Cauda epididymal plasma and seminal vesicle fluid shared at least two antigens not present in blood serum. These antigens in cauda epididymal plasma coated the sperm cell and probably were secreted by the caput epididymidis. Coating antigens were more tightly bound to ejaculated spermatozoa than to spermatozoa from the cauda epididymidis.

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A. G. HUNTER, W. L. JOHNSON, L. D. S. BARKER, M. L. FAHNING and R. H. SCHULTZ

Summary.

The seminal vesicle of the bat (Myotis lucifugus) contained a protein toxic to mice and rabbits but not to bats. This protein was precipitated with ammonium sulphate, non-dialysable, inactivated by papain and relatively heat stable. The lethal action was caused by hypotension due to a general relaxant effect on smooth muscle. Epinephrine only momentarily elevated blood pressure. The toxin had no effect on electrical transmission along the motor-nerve axon and across the neuromuscular junction. Haematocrit values increased significantly after bat seminal vesicle was injected, while a highly significant (P> 0·01) decrease in the proportion of circulating lymphocytes and a highly significant (P>0·01) increase in proportion of circulating heterophils occurred. Isolated mouse duodenum and uterine preparations showed a diminution in contraction frequency and a decrease in muscle tone in the presence of the toxin. This was reversible by washing the toxin from the system.

The hypothesis was proposed that this seminal vesicle protein enters the female bat during copulation, blocks sperm transport, and alters the phagocytic system, thus allowing bat spermatozoa to remain in the female reproductive tract over an extended period of time.

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A. G. HUNTER, L. D. S. BARKER, W. L. JOHNSON, M. L. FAHNING and R. H. SCHULTZ

Summary.

The antigenicity of male bat reproductive organs was studied using agar-gel diffusion. Four precipitin lines formed with testis and anti-testis, six lines with epididymis and anti-epididymis, and six lines with ampulla and anti-ampulla sera. Tissue extracts of liver, spleen, heart and uterus cross-reacted with the three antisera to produce three lines. Ampulla, epididymis and testis possessed at least one, three and one organ-specific antigens, respectively.

Nine proteins were detected in the seminal vesicles by agar-gel electrophoresis. One of these possessed potent toxic properties when injected into rabbits and mice. The toxic protein was isolated by zonal electrophoresis and by chromatography on Sephadex G-200. It migrated electrophoretically as a pre-albumin, had a molecular weight of approximately 44,600 and an LD50 value of 162μg/kg. The relationship between this protein and the unique phenomenon of bat sperm survival is unknown.