https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:27632 Sat 24 Mar 2018 07:34:05 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:41763 p < 0.001), increased further following acrosome reaction (p < 0.01), and was localized to the equatorial region of the sperm head. Testisin was also detected in luminal fluid within the caput and corpus regions of the epididymis, epididymal spermatozoa, and epididymal epithelial cells. Testisin formed several multiprotein complexes; co‐immunoprecipitation revealed interactions of testisin with a multitude of zona pellucida‐binding proteins, including ZPBP, ZAN, acrosin, several heat‐shock proteins, and components of the TCP1 complex. Conclusion: Testisin appears to form part of the zona pellucida‐binding complex in stallion spermatozoa and may be involved in the proteolytic cascade that prepares the sperm surface for interaction with the oocyte.]]> Fri 12 Aug 2022 11:49:34 AEST ]]>