[Fractionation of alpha-L-fucosidases from pig kidney by gel filtration and isoelectric focusing].

Molecular weights of alpha-L-fucosidases I and II were found to be about 200 000 and 140 000, respectively, by means of gel filtration. Unlike alpha-L-fucosidase I, alpha-L-fucosidase II were capable of binding with Sephadex for the expense of non-specific adsorption, which makes possible to purify alpha-L-fucosidase II from ballast protein under certain conditions. Some problems concerning interrelation of both fucosidases forms are discussed and data on isoelectric focusing are given, which suggest the heterogeneity of both alpha-L-fucosidases.