A genomic library of Bifidobacterium bifidum constructed in Escherichia coli was screened for the ability to hydrolyze the ␣-(132) linkage of 2-fucosyllactose, and a gene encoding 1,2-␣-L-fucosidase (AfcA) was isolated. The afcA gene was found to comprise 1,959 amino acid residues with a predicted molecular mass of 205 kDa and containing a signal peptide and a membrane anchor at the N and C termini, respectively. A domain responsible for fucosidase activity (the Fuc domain; amino acid residues 577 to 1474) was localized by deletion analysis and then purified as a hexahistidine-tagged protein. The recombinant Fuc domain specifically hydrolyzed the terminal ␣-(132)-fucosidic linkages of various oligosaccharides and a sugar chain of a glycoprotein. The stereochemical course of the hydrolysis of 2-fucosyllactose was determined to be inversion by using 1 H nuclear magnetic resonance. The primary structure of the Fuc domain exhibited no similarity to those of any glycoside hydrolases (GHs) but showed high similarity to those of several hypothetical proteins in a database. Thus, it was revealed that the AfcA protein constitutes a novel inverting GH family (GH family 95).␣-L-Fucosyl residues are frequently found at the nonreducing termini of various glycoconjugates, including blood group substances, milk oligosaccharides, gastric and submaxillary mucins, and serum glycoproteins (30, 37). The results of recent studies indicate that such terminal fucosyl residues attached by

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The strain changes of the central part of the anterior talofibular ligament (ATFL), the posterior talofibular ligament (PTFL), the calcaneofibular ligament (CFL), and the tibiocalcaneal ligament (TCL) were measured simultaneously for a full range of ankle motion. Twelve fresh frozen amputated ankles were used. To measure the strain changes of the ligaments, a Galium-Indium-filled silastic strain transducer was implanted in the center of each ligament. The zero strain reference was determined immediately after the measurement of strain changes in five of the 12 ankles by tensile testing of each bone-ligament-bone preparation. The maximum strain change of the ATFL, the PTFL, the CFL and the TFL were 7.9%, 5.9%, 5.3% and 5.2%, respectively. The ATFL was elongated in plantar flexion and shortened in dorsiflexion. The PTFL and the CFL were shortened in plantar flexion and elongated in dorsiflexion. The TCL was the longest around the neutral position and became shorter in planter flexion and dorsiflexion. The results showed that the ATFL was taut in plantar flexion over 16.2 degrees, the PTFL and the CFL were taut in dorsiflexion over 18 degrees and 17.8 degrees respectively, and the TCL was taut between 9.5 degrees of dorsiflexion and 9.5 degrees of plantar flexion. The length change pattern was different among the ankle ligaments, although there was only a slight difference between that of the PTFL and the CFL. This study provides fundamental data useful in studying ankle ligament reconstruction.