The primary structure of BSP‐30K, a major lipid‐, gelatin‐, and heparin‐binding glycoprotein of bovine seminal plasma
- 2 December 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 399 (1-2) , 147-152
- https://doi.org/10.1016/s0014-5793(96)01310-5
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.Keywords
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