The primary structure of BSP‐30K, a major lipid‐, gelatin‐, and heparin‐binding glycoprotein of bovine seminal plasma

FEBS Letters

Mann, Karlheinz¹  Töpfer-Petersen, Edda³  Sanz, Libia³  Calvete, Juan J.³  Raida, Manfred² 

[1] Max-Planck-Institut für Biochemie, Martinsried, Germany;Niedersächsisches Institut für Peptid-Forschung GmbH, Hannover, Germany;Institut für Reproduktionsmedizin, Tierärztliche Hochschule Hannover, Bünteweg 15, 30559 Hannover-Kirchrode, Germany

关键词: Protein BSP-30K;    Heparin-binding protein;    Bovine seminal plasma;    Primary structure;    O-Glycosylation;    Fibronectin type II domain;   

DOI  :  10.1016/S0014-5793(96)01310-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown