Characterization of human alpha-galactosidase A and B before and after neuraminidase treatment
| Autor: | Su-Chen Li, Yu-Teh Li, Michelle D'Urso, Gianfranco Di Matteo, Giovanni Romeo |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Starch
Clostridium perfringens Serum albumin Neuraminidase Chromatography DEAE-Cellulose chemistry.chemical_compound Animals Humans chemistry.chemical_classification Chromatography biology Isoelectric focusing Substrate (chemistry) Serum Albumin Bovine General Medicine Molecular biology Galactosidases Isoenzymes Transformation (genetics) Electrophoresis Kinetics Enzyme chemistry Biochemistry Liver biology.protein Chromatography Gel Cattle Hydroxyapatites Isoelectric Focusing |
| Zdroj: | Biochimica et biophysica acta. 391(2) |
| ISSN: | 0006-3002 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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