Echinococcus granulosus, E. multilocularis and mammalian liver-type alkaline phosphatases: a comparative study
| Autor: | Philippe Lawton, Marie-Elisabeth Sarciron, Anne-Françoise Pétavy |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
Sheep Physiology Phosphatase Phenylalanine Biology Alkaline Phosphatase biology.organism_classification Biochemistry Echinococcus Enzyme Activation chemistry.chemical_compound Enzyme Liver chemistry Animals Alkaline phosphatase Parasite hosting Enzyme Inhibitors PMSF Echinococcus granulosus Molecular Biology |
| Zdroj: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 112:295-301 |
| ISSN: | 1096-4959 |
| Popis: | The alkaline phosphatases (EC 3.1.3.1) from Echinococcus granulosus and E. multilocularis (Cestoda) were compared to each other and to a liver-type enzyme. The purified proteins (210 and 220 kDa, respectively) had a tetrameric structure composed of 4, 56/53 kDa subunits. Enzymatic removal of their N -linked sugar moieties abolished the differences in their apparent molecular weight under reducing conditions. After phase separation in Triton X-114, the E. multilocularis enzyme was the most amphiphilic, and treatment with PI-PIC reduced the amount of the parasite alkaline phosphatases that were in a hydrophobic form by about 50%. Both parasite enzymes were highly resistant to heat denaturation and insensitive to the inhibitors l -phenylalanine and l -leucine. In addition, l -homoarginine, levamisole and ZnCl 2 can be used to differentiate the parasite and mammalian liver-type enzymes from each other. The Echinococcus alkaline phosphatases have original biochemical properties when compared to the mammalian liver-type enzyme. |
| Databáze: | OpenAIRE |
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