Purification and partial characterization of the 17 kDa sperm coating protein from boar seminal plasma
Language English Country United States Media print
Document type Journal Article
PubMed
1418985
DOI
10.1002/mrd.1080330208
Knihovny.cz E-resources
- MeSH
- Acrosome physiology MeSH
- Antigens, Surface immunology isolation & purification MeSH
- Ejaculation MeSH
- Epididymis MeSH
- Sperm Capacitation MeSH
- Antibodies, Monoclonal immunology MeSH
- Mice MeSH
- Organ Specificity MeSH
- Swine metabolism MeSH
- Semen chemistry MeSH
- Zona Pellucida metabolism MeSH
- Animals MeSH
- Check Tag
- Male MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Antigens, Surface MeSH
- Antibodies, Monoclonal MeSH
Sperm coating proteins of 16, 17, and 19 kDa have been purified from boar seminal plasma. The 17 kDa protein has been identified as an antigen recognized by monoclonal antibody ACR.3 and is thus identical to low molecular mass zona pellucida binding protein from boar spermatozoa (Moos et al., 1990). The 17 and 19 kDa proteins are glycosylated and tend to form hetero-complexes. The 17 kDa ACR.3 antigen is sequentially released from the sperm cell surface during capacitation and, after induction of the acrosome reaction, the 16 kDa form was also observed. Immunocytochemical studies on boar reproductive tissues have suggested that the seminal vesicle epithelium may be the source of these proteins.
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