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• W2078358908 abstract "In the bovine, seminal plasma heparin‐binding proteins bind to sperm lipids containing the phosphorylcholine group and mediate the capacitating effects of heparin‐like glycosaminoglycans during sperm residence in the female genital tract. We report the characterization of heparin‐ and phosphorylcholine‐binding proteins of stallion and boar seminal plasma. orse eminal lasma proteins HSP‐1 and HSP‐2, and boar protein pB1, belong to the same family as the bull heparin‐ and phosphorylcholine‐binding proteins BSP‐A 1/2 , BSP‐A 3 , and BSP‐30K. We have determined the amino acid sequence and posttranslational modifications of boar glycoprotein pB1. It contains 105 amino acids arranged into a mosaic structure consisting of a N‐terminal 18‐residue O ‐glycosylated polypeptide followed by two tandemly organized 40–45‐residue fibronectin type II domains. pB1 displays 60–65% amino acid sequence similarity with its equine and bovine homologues. However, in their respective seminal plasmas, the BSP and the HSP proteins associate into 90–150‐kDa oligomeric complexes, whereas pB1 forms a 35–40‐kDa complex with spermadhesin AQN‐1. In addition, pB1 appears to be identical to the recently described leukocyte adhesion regulator of porcine seminal fluid pAIF‐1. Our results tie in with the hypothesis that homologous proteins from different mammalian species may display distinct biological activities, which may be related to species‐specific aspects of sperm physiology." @default.
• W2078358908 created "2016-06-24" @default.
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• W2078358908 date "1997-04-28" @default.
• W2078358908 modified "2023-10-18" @default.
• W2078358908 title "Isolation and characterization of heparin‐ and phosphorylcholine‐binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1" @default.
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• W2078358908 doi "https://doi.org/10.1016/s0014-5793(97)00344-x" @default.
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