Abstract Background: Acrosin (ACR) is one of the most important proteases in the mammalian sperm head, located within the acrosome of human spermatozoa. ACR is a proteolytic enzyme that may hydrolyze the zona pellucida in oocytes. Following its release from the acrosome, it attaches to the zona pellucida of the egg and creates small openings in the zona pellucida, allowing the sperm to enter and fertilize the egg. Objective: It was the isolation and purification of the ACR from a human seminal fluid of infertile patients and the study of the optimal conditions required for the partially purified enzyme. Materials and Methods: Include the isolation and purification of the ACR from a human seminal fluid of infertile patients using a variety of biotechniques, such as ion-exchange chromatography, where one highly active primary peak is separated by the diethylaminoethyl cellulose (DEAE-C) ion-exchange technique, dialysis, and sedimentation with 65% ammonium sulfate. Results: A major protein bundle was separated with strong activity for the ACR with a 58% recovery rate of the enzyme. optimal conditions determined for the partially purified enzyme, the highest activity was for reaction time at (9 min), (pH = 7.5), enzyme concentration (500 ng/mL), substrate concentration (60 mmol/L), temperature (37°C), V max (21.23 μmol/min), and K m (19.12 mmol/L), respectively, using the Lineweaver–Burk plot. Molecular weight of ACR partially purified was estimated a 66-kDa by using sodium dodecyl sulfate-polyacrylamide gel electrophoresis technique. Conclusion: Low levels of ACR appear to be linked to infertility and subfertility. Thus, measuring ACR activity is a viable method for assessing the fertilizing potential of human spermatozoa.
Shahadha et al. (Thu,) studied this question.