## Abstract The proteolytic action of boar sperm acrosin on its natural substrate, the zona pellucida, was investigated. Acrosin exhibited substrate specificity for the zona pellucida and differentially hydrolyzed the glycoprotein families composing the zona pellucida. In contrast to acrosin, tryps
Proteolysis of the zona pellucida by acrosin: The nature of the hydrolysis products
β Scribed by Urch, Umbert A. ;Wardrip, Nathan J. ;Hedrick, Jerry L.
- Publisher
- John Wiley and Sons
- Year
- 1985
- Tongue
- English
- Weight
- 496 KB
- Volume
- 236
- Category
- Article
- ISSN
- 0022-104X
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β¦ Synopsis
Boar sperm acrosin was previously shown to hydrolyze the porcine zona pellucida in a specific and limited fashion. The action of acrosin on its presumed physiological substrate was investigated further in terms of the hydrolysis products formed. Peptide mapping experiments of zona pellucida glycoprotein families using acrosin demonstrated the formation of several products 2-4K smaller than the original susceptible families. When zona pellucida hydrolysates were examined with gel filtration, the hydrolysis products were associated in large macromolecular aggregates. These observations suggest that zona pellucida solubilization by acrosin may not be a relevant criterion for assessing acrosin's role in sperm penetration of the zona pellucida.
In previous reports, the porcine zona pellucida (ZP) was described as a specific substrate for boar sperm acrosin, and the susceptible glycoprotein components of the ZP were hydrolyzed in a selective fashion (Urch et al., '82, '85; Hedrick et al., '85; Urch, '85). Defining the hydrolytic mechanism of ZP hydrolysis by acrosin may assist in defining the sequence of chemical events involved in the
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