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- W2134964111 abstract "Examination of the role of carbohydrates in specific recognition between spermatozoa and zona pellucida has focussed on understanding the interaction of sperm hydrolases or lectin-like molecules with zona pellucida ligands. To elucidate the role of specific spermatozoan hydrolases in gamete interaction, rabbit testis beta-galactosidase and arylsulfatase A were purified, characterized, and localized in spermatozoa. beta-Galactosidase and arylsulfatase A co-purified after affinity, size, or reverse-phase chromatography. N-Terminal amino acid analysis and enzymatic characterization suggested that neither enzyme is a testis-specific isozyme. Size chromatography indicated that both enzymes aggregated into macromolecular complexes at pH 4.0, while both dissociated at pH 8.0. beta-Galactosidase and arylsulfatase A co-localized on the sperm surface and in the acrosome and postacrosomal regions of spermatozoa. Throughout the zona-induced acrosome reaction, both enzymes remained associated with the detached acrosomal cap and postacrosomal region of acrosome-reacted spermatozoa. Because the acrosome is an acidic subcellular compartment, internal beta-galactosidase and arylsulfatase A are probably aggregated in acrosome-intact spermatozoa and dissociate as they are exposed to pH increases during the acrosome reaction." @default.
- W2134964111 created "2016-06-24" @default.
- W2134964111 creator A5007261565 @default.
- W2134964111 creator A5068729549 @default.
- W2134964111 date "1992-03-01" @default.
- W2134964111 modified "2023-10-15" @default.
- W2134964111 title "Characterization of Rabbit Testis β-Galactosidase and Arylsulfatase A: Purification and Localization in Spermatozoa during the Acrosome Reaction1" @default.
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- W2134964111 doi "https://doi.org/10.1095/biolreprod46.3.366" @default.
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