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• W1987128839 abstract "BSP‐30K is a major acidic glycoprotein of bovine seminal plasma. It displays heparin‐, gelatin‐, and phospholipid‐binding activities. BSP‐30K binds to spermatozoa upon ejaculation and is thought to play a role in sperm capacitation. We have determined its amino acid sequence, disulfide bonds, and O ‐glycosylation sites. BSP‐30K consists of 158 amino acids arranged in a mosaic structure. BSP‐30K has a unique 48‐residue N‐terminal extension which includes three 7–8‐ amino acid repeats and the six O ‐glycosylated threonine residues. The polypeptide stretch 49–71 is homologous to type ‘A’ domains found in heparin‐binding proteins from other mammalian species. The C‐terminal portion of BSP‐30K is organized in a tandem of 40–44‐residue domains each sharing the consensus pattern of the gelatin‐binding fibronectin type II module. The mosaic structure of BSP‐30K suggests that this glycoprotein might be a factor contributing to the different sperm‐capacitatiog effects exerted by heparin in different mammalian species." @default.
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• W1987128839 date "1996-12-09" @default.
• W1987128839 modified "2023-10-14" @default.
• W1987128839 title "The primary structure of BSP-30K, a major lipid-, gelatin-, and heparin-binding glycoprotein of bovine seminal plasma" @default.
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• W1987128839 doi "https://doi.org/10.1016/s0014-5793(96)01310-5" @default.
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