The complete primary structure of three isoforms of a boar sperm-associated acrosin inhibitor

• Published in: FEBS letters 1992-02, Vol.297 (1), p.147-150
• Main Authors: Jonáková, Věra, Calvete, Juan J., Mann, Karlheinz, Schäfer, Wolfram, Schmid, Erich R., Töpfer-Petersen, Edda
• Format: Article
• Language: English
• Subjects: Acrosin - antagonists & inhibitors; acrosin inhibitor; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; association; Biological and medical sciences; Boar acrosin isoinhibitor; Chromatography, High Pressure Liquid; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Hydrolases; Male; Mass spectrometry; Molecular Sequence Data; pigs; Semen - metabolism; Sequence Alignment; Serine Proteinase Inhibitors - genetics; spermatozoa; Spermatozoa - metabolism; Swine
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(92)80347-J

Acrosin inhibitors of seminal vesicle origin, after binding to their acceptor molecules on the anterior part of ejaculated sperm, are thought to be important capacitation factors, protecting zona binding sites during sperm uterine passage, and then dissociating to allow sperm binding to the zona pellucida of the oocyte. Each species so far tested possess an heterogeneous population of isoinhibitors which may display overlapping but not identical biological functions. Here we report the complete primary structure of three isoforms of a boar sperm-associated acrosin inhibitor, whose sequences are 90% identical to the seminal plasma counterpart. Despite this high analogy, the differences between the sperm-associated and the seminal plasma inhibitors may confer to them different physico-chemical properties which are postulated to be of functional importance.