Purification of α-l-fucosidase from various sources by affinity chromatography
| Autor: | A. Levy-Benshimol, Leonard Warren, Clayton A. Buck, Ram Sarup Jain, Robert L. Binder |
|---|---|
| Rok vydání: | 1977 |
| Předmět: |
Male
Clostridium perfringens Disaccharidases medicine.disease_cause Biochemistry Chromatography Affinity Analytical Chemistry Sepharose Affinity chromatography Horseshoe Crabs medicine Animals Fucosidase Pyrans Epididymis alpha-L-Fucosidase chemistry.chemical_classification Chromatography biology Organic Chemistry Proteolytic enzymes General Medicine Hydrogen-Ion Concentration biology.organism_classification Rats Kinetics Enzyme chemistry Limulus Yield (chemistry) biology.protein |
| Zdroj: | Journal of Chromatography A. 139:283-290 |
| ISSN: | 0021-9673 |
| DOI: | 10.1016/s0021-9673(00)89322-x |
| Popis: | An affinity column for α- l -fucosidases was constructed by linking p -aminophenyl 1-thio-α- l -fucopyranoside to Sepharose 4B through linkers of succinyl 3,3′-diamino-dipropylamine. Excellent purification of α- l -fucosidase from rat epididymis, Clostridium perfringens and Limulus polyphemus (horse shoecrab) could be effected in one step with good yield. An affinity column purification step can be introduced at any point in published purification procedures. The purified enzyme is essentially free of other glycosidases and proteolytic enzymes. The column material is stable and can be reused for at least two years. |
| Databáze: | OpenAIRE |
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