Androgen-regulated proteins of rat seminal vesicle secretion constitute a structurally related family present in the copulatory plug.
All the major androgen-regulated secretory proteins of rat seminal vesicles have been purified in high yield from polyacrylamide gels using electroelution. In the process a sixth previously undocumented protein has been identified. Amino acid compositions of all the proteins are very similar and highly unusual, being high in lysine and arginine, and with 40-50% of the residues accounted for by serine, glycine and glutamate/glutamine. N-Terminal amino acid sequences for 3 of the proteins show that they are clearly the products of related genes. At least one of the other proteins is N-terminally blocked in vivo. Antibodies specific for each protein have been raised and provide evidence of structural similarity between the proteins. The antibodies were also used in immunofluorescence histochemistry with the rat copulatory plug, showing for the first time that all the major proteins of seminal vesicle secretion are components of this reproductive structure.
S E
SE
Fawell
D J
DJ
Pappin
C J
CJ
McDonald
S J
SJ
Higgins
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D003307:Copulation; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000276:immunology; D005455:Fluorescent Antibody Technique; D006651:Histocytochemistry; D007106:Immune Sera / Q000276:immunology; D008297:Male; D011506:Proteins / Q000032:analysis* / Q000276:immunology / Q000502:physiology; D051381:Rats; D011919:Rats, Inbred Strains; D012669:Seminal Vesicles / Q000378:metabolism*
D000596:Amino Acids; D000939:Epitopes; D007106:Immune Sera; D011506:Proteins