The acid alpha -L-fucosidase is usually found as a soluble component of lys
osomes where fucoglycoconjugates are degraded. In the present investigation
, we have demonstrated the existence of a cell surface protein with enzymat
ic alpha -L-fucosidase activity that crossreacts specifically with a rabbit
anti-(alpha -L-fucosidase) Ig. By different approaches, this alpha -L-fuco
sidase, which represents 10-20% of the total cellular fucosidase activity,
was detected in all the tested human cells (hemopoietic, epithelial, mesenc
hymal). Two bands of approximate to 43-49 kDa were observed, although theor
etical data support the possibility of having the same genetic origin that
the known 50 to 55-kDa M-r alpha -L-fucosidase. We speculate about an alter
native traffic pathway for the plasma membrane alpha -L-fucosidase to work
on the rapid turnover of glycoproteins.