Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2025 Jun 17:15:1596356.
doi: 10.3389/fcimb.2025.1596356. eCollection 2025.

Extraction, purification, biological effects and applications of acrosin: a review

Affiliations
Review

Extraction, purification, biological effects and applications of acrosin: a review

Run Quan et al. Front Cell Infect Microbiol. .

Abstract

Acrosin is a proteolytic enzyme in the sperm acrosome that can stimulate sperm to penetrate the zona pellucida, causing the fertilization of the oocyte. Its activity is a crucial indicator of the sperm's fertilization ability, which is critical in mammalian and human reproduction. However, there exists a lack of a comprehensive review of acrosin. In this study, we compared the extraction methods of acrosin, including acid extraction, buffer extraction, and saline extraction. The main methods for purifying acrosin, such as ammonium sulfate precipitation, ultrafiltration, dialysis, gel filtration chromatography, ion-exchange chromatography, and affinity chromatography, are reviewed. In addition, a detailed overview of the biological functions, inhibitors and applications of acrosin are outlined. This study provides methods for the extraction and purification of acrosin and some theoretical basis for the study of its properties. This provides a reference for further research on acrosin.

Keywords: acrosin; acrosin inhibitor; enzymatic properties; extraction; purification; reproduction.

PubMed Disclaimer

Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

Figure 1
Figure 1
Extraction and purification process of acrosin and proacrosin.
Figure 2
Figure 2
3D structure and active site of acrosomal enzymes from different animals Detailed view of the active sites with acrosin is displayed on the ellipse. The yellow area indicates the active site, and the magenta dashed line indicates the force of interaction between the active site and the ligand. (A) Rabbit; (B) Pig; (C) Rat; (D) Human; (E) Wild turkey; (F) Quail (Bateman et al., 2024).
Figure 3
Figure 3
Main purification methods of acrosin.

Similar articles

References

    1. Adekunle A. O., Arboleda C. E., Zervos P. H., Gerton G. L., Teuscher C. (1987). Purification and initial characterization of Guinea pig testicular acrosin. Biol. Reproduction. 37, 201–210. doi: 10.1095/biolreprod37.1.201 - DOI - PubMed
    1. Adeniran A. J., Shoshani I., Minuth M., Awad J. A., Elce J. S., Johnson R. A. (1995). Purification, characterization, and N-terminal amino acid sequence of the adenylyl cyclase-activating protease from bovine sperm. Biol. Reproduction. 52, 490–499. doi: 10.1095/biolreprod52.3.490 - DOI - PubMed
    1. Adham I. M., Nayernia K., Engel W. (1997). Spermatozoa lacking acrosin protein show delayed fertilization. Mol. Reprod. Dev. 46, 370–376. doi: 10.1002/(sici)1098-2795(199703)46:3<370::Aid-mrd16>3.0.Co;2-2 - DOI - PubMed
    1. Adham I. M., Schlsser M., Engel W. (2013). Acrosin. Encyclopedia Mol. Medicine. 3, 2731–2735. doi: 10.1016/B978-0-12-382219-2.00602-5 - DOI
    1. Adham I. M., Szpirer C., Kremling H., Keime S., Szpirer J., Levan G., et al. (1991). Chromosomal assignment of four rat genes coding for the spermatid-specific proteins proacrosin (ACR), transition proteins 1 (TNP1) and 2 (TNP2), and protamine 1 (PRM1). Cytogenetics Cell Genet. 57, 47–50. doi: 10.1159/000133113 - DOI - PubMed

LinkOut - more resources