The purification and properties of β-galactosidase from bovine testes
JJ Distler, GW Jourdian - Journal of Biological Chemistry, 1973 - ASBMB
A β-galactosidase was purified 600-fold from bovine testes by ammonium sulfate
precipitation, acetone fractionation, and affinity chromatography on agarose substituted with
terminal thio-β-galactopyranosyl residues. The preparation was devoid of protease, α-
fucosidase, α-mannosidase, β-glucosidase, β-glucuronidase, and hyaluronidase activities. A
wide variety of compounds containing terminal nonreducing galactose residues were
hydrolyzed by the enzyme, including proteoglycans, glycoproteins, gangliosides …
precipitation, acetone fractionation, and affinity chromatography on agarose substituted with
terminal thio-β-galactopyranosyl residues. The preparation was devoid of protease, α-
fucosidase, α-mannosidase, β-glucosidase, β-glucuronidase, and hyaluronidase activities. A
wide variety of compounds containing terminal nonreducing galactose residues were
hydrolyzed by the enzyme, including proteoglycans, glycoproteins, gangliosides …