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  • Title: Affinity chromatography of bull seminal proteins on mannan-Sepharose.
    Author: Liberda J, Ryslavá H, Jelínková P, Jonáková V, Tichá M.
    Journal: J Chromatogr B Analyt Technol Biomed Life Sci; 2002 Nov 25; 780(2):231-9. PubMed ID: 12401348.
    Abstract:
    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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