Gene expression in bovine seminal vesicles: Genexpression in der Bullenbläschendrüse

Abstract

Seminal vesicle secretion contributes significantly to the proteins of bovine seminal plasma. The following proteins from bull seminal vesicle were isolated and characterized: major protein (PDC 109), the basic proteins BUSI II, RNAse BS1, protein P6 and seminal antimicrobial protein (SAP). Using antibodies against the proteins BUSI II, RNAse BS1, SAP and major protein, the seminal vesicle epithelium was identified as the source of the respective antigens. The biosynthesis of bovine seminal vesicle secretory proteins was studied by cell free translation of poly (A)-RNA from seminal vesicles and the respective mRNAs were characterized by cDNA cloning. Recombinant clones (103) of a cDNA library of bull seminal vesicle poly (A) + RNA were screened by colony hybridisation using radioactively labelled synthetic probes. The respective clone containing the longest cDNA insert was sequenced. In case of major protein the Mr of the 134 amino acid residue precursor polypeptide was 15,480 as deduced from direct mRNA sequencing. The precursor sequence of 25 amino acid residues has a hydrophobic character and very likely constitutes a signal peptide, directing the protein towards the secretory pathway. The deduced amino acid sequence contained no consensus sequence indicative of N-glycosylation.