Purification and partial characterization of the 17 kDa sperm coating protein from boar seminal plasma
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
1418985
DOI
10.1002/mrd.1080330208
Knihovny.cz E-zdroje
- MeSH
- akrozom fyziologie MeSH
- antigeny povrchové imunologie izolace a purifikace MeSH
- ejakulace MeSH
- epididymis MeSH
- kapacitace spermií MeSH
- monoklonální protilátky imunologie MeSH
- myši MeSH
- orgánová specificita MeSH
- prasata metabolismus MeSH
- sperma chemie MeSH
- zona pellucida metabolismus MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- myši MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- antigeny povrchové MeSH
- monoklonální protilátky 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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