We previously demonstrated polymorphism of a mouse salivary protein which, because of its ability to bind androgen, we designated androgen binding protein (ABP) and its structural gene, Androgen binding protein (Abp). This report describes the purification of salivary ABP and presents the amino acid composition of its subunits. Using an antibody raised against the purified protein, we demonstrated the presence of cross-reactive material (CRM) in mouse parotid, submaxillary, sublingual, and prostate glands by double immunodiffusion. Immunohistochemical detection of proteins on electroblots of polyacrylamide electrophoresis and isoelectric focusing gels, however shows that the prostate CRM is a protein with electrophoretic and isoelectric focusing behavior distinct from that of salivary ABP isoproteins. Because the DBA/2J strain has a variant of salivary ABP, that strain was analyzed to determine if a prostate ABP-CRM variant was present. The approach was hampered by an inability to detect CRM in the prostates of DBA/2J mice. Prostate CRM was detected, however, in some progeny from repeated backcrosses of DBA/2J × C3H/St hybrids to the C3H/St and DBA/2J parental strains. The prostate CRM detected in samples from animals heterozygous for salivary Abp appears to be identical to C3H/St prostate CRM, suggesting that the gene controlling prostate ABP-CRM is related to, but distinct from, Abp. The reason for reduced or absent CRM in the prostates of DBA/2J males is unknown but this finding suggests that there are strain-related differences in the expression of this prostate protein.
androgen binding proteins mouse salivary proteins mouse prostate Western transfer