Affinity chromatography of bull seminal proteins on mannan-Sepharose
Jazyk angličtina Země Nizozemsko Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
12401348
DOI
10.1016/s1570-0232(02)00521-4
PII: S1570023202005214
Knihovny.cz E-zdroje
- MeSH
- chromatografie afinitní metody MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- mannany chemie MeSH
- proteiny chemie izolace a purifikace MeSH
- sefarosa chemie MeSH
- sekvence aminokyselin MeSH
- skot MeSH
- sperma chemie MeSH
- zvířata MeSH
- Check Tag
- mužské pohlaví MeSH
- skot MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- mannany MeSH
- proteiny MeSH
- sefarosa MeSH
The interaction of bull seminal plasma proteins and sperm with mannan was investigated using an enzyme-linked binding assay (ELBA). A high mannan-binding activity was found in the protein fraction interacting with heparin. Mannan binding to seminal plasma proteins was inhibited by D-mannose and D-fructose, but not by D-mannose-6-phosphate, D-glucose-6-phosphate, ovalbumin and ovomucoid. Mannan inhibited the binding of bovine zona pellucida glycoproteins both to bull sperm and seminal plasma proteins. Yeast mannan immobilized to divinyl sulfone-activated Sepharose was used for the isolation of mannan-binding proteins. The protein components of this fraction were identified on the basis of relative molecular mass determination and N-terminal amino acid sequencing: RNAase dimer, PDC-109 and a protein homologous to BSP-30K (relative molecular mass 14,500). The isolated proteins were characterized by a high zona pellucida binding activity.
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