Immunological Identification of Seminaiplasmin in Tissue Extracts of Sex Glands of Bull

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Abstract
IgG antibodies raised against highly purified, homogeneous seminalplasmin, an antimicrobial protein of bovine seminal plasma indicated that bovine ampullae, gland vesicularis and corpus prostate, but not testes and epididymis, contain seminalplasmin. The content as estimated by radioimmunoassay employing 125I-seminalplasmin was: ampullae, 267 .+-. 13; gland vesicularis, 275 .+-. 14; and corpus prostate, 445 .+-. 22 .mu.g/g wet wt of the tissue. Seminalplasmin, as characterized by high-performance liquid chromatography and in vivo inhibition of RNA synthesis in Escherichia coli, was isolated from gland vesicularis. The seminalplasmin content of bovine seminal plasma was 1%. A chymotryptic peptide of seminalplasmin comprising residues 1-13 from the amino terminus competed with 125I-seminalplasmin for binding to anti-seminalplasmin IgG.

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