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Western analysis revealed that the sperm\u2010associated \u03b1\u2010<jats:sc>L<\/jats:sc>\u2010fucosidase is present as two isoforms (Mr \u223c49 and 56\u2009kDa), whereas the cauda fluid \u03b1\u2010<jats:sc>L<\/jats:sc>\u2010fucosidase shows a single band at 50\u2009kDa. \u03b1\u2010<jats:sc>L<\/jats:sc>\u2010Fucosidase activity was detected using the fluorogenic substrate 4\u2010MU\u2010FUC. Of the total \u03b1\u2010<jats:sc>L<\/jats:sc>\u2010fucosidase activity recovered in the cauda epididymal contents, 74% was found in the cell\u2010free cauda fluid and about 7% was found in sperm cells. During capacitation or permeabilization, cryptic intracellular stores of soluble enzyme were released to the supernatant, while leaving bound enzyme concentrated within the small volume of sperm. Moreover, membrane\u2010associated enzyme activity was still detectable in acrosome\u2010reacted cells. Immunofluorescence studies support the presence of \u03b1\u2010<jats:sc>L<\/jats:sc>\u2010fucosidase (originally localizing at the acrosomal area) at the equatorial segment after the acrosome reaction. \u03b1\u2010<jats:sc>L<\/jats:sc>\u2010Fucosidase activity of both cauda fluid and sperm at 37\u00b0C, 5% CO<jats:sub>2<\/jats:sub> was relatively stable and detectable up to 72\u2009hr. The stability and appearance of mouse sperm\u2010associated \u03b1\u2010<jats:sc>L<\/jats:sc>\u2010fucosidase in the equatorial segment after the acrosome reaction suggest that \u03b1\u2010<jats:sc>L<\/jats:sc>\u2010fucosidase may be involved in sperm\u2013egg interaction. Mol. Reprod. 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