Abstract
Sperm motility inhibiting factor (SMIF) has been isolated from boar seminal plasma by acetone fractionation and thin-layer chromatography on silica gel. Low molecular weight (5700 Da), maximal absorbance at 220 nm, significant thermostability, positive ninhidrin reaction and dominating acidic amino acid residues indicate the SMIF is a peptide and anionic. SMIF showed non-species-specific inhibition of sperm motility in microscopic studies. An antigenic species-specificity of SMIF was demonstrated. Immunofluorescence confirmed that the peptide was secreted by epithelial cells of the vesicle glands. No fluorescence was observed in other tissues of the boar's reproductive system. SMIF was associated with macromolecular protein fractions of seminal plasma and vesicle fluid. Whole plasma of boar semen showed a modulating effect on the inhibiting activity of SMIF. Adenosine receptor antagonist, in 10 mM concentration, as well as caffeine and theophylline, decreased the inhibitory activity of the peptide on sperm motility. SMIF significantly decreased the adenosine 5′,-triphosphate content of spermatozoa and inhibited growth of Gram-positive bacterial species. The lytic activity of SMIF against Micrococcus lysodeikticus (luteus), observed by a turbidimetric method, suggests that SMIF could interact with the spermatozoa membrane. The results suggest that SMIF is a regulating peptide of boar seminal plasma.
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