title: Characterization of human alpha-galactosidase A and B before and after neuraminidase treatment.
abstract: It has been previously reported that following neuraminidase treatment alpha-galactosidase A is converted into the B form, as revealed by electrophoresis. By a variety of techniques such as isoelectrofocusing, DEAE-chromatography and by enzyme kinetic parameters, no conversion of alpha-galactosidase A into B, or the reverse, could be detected after neuraminidase treatment. Only an apparent transformation of alpha-galactosidase A into B was revealed by Cellogel electrophoresis. In addition, a discrepancy was noticed between the pattern of electrophoretic migration on starch gel and Cellogel and the net electrical charges of the two alpha-galactosidases as deduced by isoelectrofocusing and DEAE-cellulose. Neuraminidase treatment did not affect the activity of alpha-galactosidase A towards the natural substrate, ceramidetrihexoside, but the activity of alpha-galactosidase B decreased by about 30% under the same conditions. The two forms of alpha-galactosidases A and B used in this study were extensively purified by classical procedures.
mesh_terms: D000818:Animals; D002417:Cattle; D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D003016:Clostridium perfringens / Q000201:enzymology; D005696:Galactosidases / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D006882:Hydroxyapatites; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009439:Neuraminidase; D012710:Serum Albumin, Bovine / Q000494:pharmacology
chemical_list: D006882:Hydroxyapatites; D007527:Isoenzymes; D012710:Serum Albumin, Bovine; D005696:Galactosidases; D009439:Neuraminidase