Purification and Some Properties of Fucosyltransferase in Human Parotid Saliva
| Autor: | A. Tsunemitsu, Tetsuo Takeshita, Satoshi Shizukuishi, Eiji Inoshita, Hiroo Tamagawa, M. Takagaki |
|---|---|
| Rok vydání: | 1987 |
| Předmět: |
Adult
0301 basic medicine Fucosyltransferase Chromatography Paper Chromatography Affinity Sepharose 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Glucoside Affinity chromatography Humans Parotid Gland Transferase Fucosidase Saliva General Dentistry Chromatography High Pressure Liquid alpha-L-Fucosidase chemistry.chemical_classification Chromatography biology Chromatofocusing Sodium Dodecyl Sulfate 030206 dentistry Fucosyltransferases 030104 developmental biology Enzyme Hexosyltransferases Biochemistry chemistry biology.protein Electrophoresis Polyacrylamide Gel |
| Zdroj: | Journal of Dental Research. 66:72-77 |
| ISSN: | 1544-0591 0022-0345 |
| DOI: | 10.1177/00220345870660011601 |
| Popis: | Fucosyltransferase was purified from human parotid saliva by affinity chromatography on GDP-hexanolamine Sepharose, followed by chromatofocusing on PBE 94 exchanger gel. The purified enzyme had the N-acetyglucosaminide alpha 1----4, the N-acetylglucosaminide alpha 1----3, and the glucoside alpha 1----3 fucosyltransferase activities. The molecular weight of the purified enzyme was estimated to be approximately 20,000. These enzyme activities showed identical pH and divalent metal ion dependencies and identical rates of inactivation upon being heated. The paper chromatographic analysis of the fucosylated products by the purified enzyme and the susceptibility of these products to linkage-specific fucosidase digestion indicated that the transferase formed the Fuc alpha 1----4GlcNAc, Fuc alpha 1----3GlcNAc, and Fuc alpha 1----3Glc linkages. |
| Databáze: | OpenAIRE |
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