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Partial Physico-Chemical and Immunological Characterization of Bovine Semen Isoantigens^{1 ,2,}

The Ohio State University and The Ohio Agricultural Research and Development Center⁴, Columbus 43210

Abstract

Antisera prepared by im semen pooled from eight bulls of four dairy breeds reacted in immunodiffusion tests to indicate that bovine semen contains at least four isoantigens. No visible precipitin reaction was observed when such sera were diffused against vesicular gland fluid, but all four antigens were present in the testicular fluid, cauda epididymal plasma, cauda epididymal sperm and caput epididymal fluid, indicating that they arise from the testes. This viewpoint was supported by the results of immunofluorescence investigations.

Bovine seminal plasma was fractionated into five protein components on a Sephadex G-200 column. One area of isoantigenicity was associated with the trailing portion of the first protein peak and another was found in the leading portion of the second peak. There was no clear association of any individual precipitin line with only one of these molecular weight regions; in fact, the observed recurrent multiplicity suggested a dependent relationship. These antigenic regions corresponded to molecular weight estimation points of 285,000 and 110,000 daltons, respectively.

The isoantigens, designated 1 to 4 in order of proximity to the antiserum well, were increasingly more heat labile and Pronase vulnerable. Isoantigen 1 was destroyed by heating at 65 C for 30 min, antigens 2 and 3 at 65 C for 15 min, while antigen 4 was destroyed by 56 C for 30 minutes. Pronase treatment appeared to destroy antigens 3 and 4. Alpha amylase failed to produce any noticeable effect on any of the antigens.

Immunological tests revealed that anti-semen antibodies were present in the reproductive fluid of two of 30 tested, untreated bulls. These antibodies, which appeared to have entered the reproductive fluid via the vesicular glands, reacted with whole or fractionated seminal plasma to produce multiple precipitin lines identical with those produced by antibodies in the experimental antisera.

¹ Approved for publication as Journal Article No. 4–76 of The Ohio Agricultural Research and Development Center, Wooster 44691.

² The cooperation of Select Sires, Inc., Plain City, OH, is gratefully acknowledged. Appreciation is also expressed to Dr. W. R. Gomes and Dr. T. M. Ludwick for their helpful suggestions.

³ Present address: Department of Animal Science, Southern University, Baton Rouge, LA 70813.

⁴ Department of Dairy Science.