Origin of intestinal disaccharidases of Ascaris suum
| Autor: | Harry W. Gentner, Gilbert A. Castro |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Hot Temperature
Swine Immunology Trehalase activity Biology Disaccharidases Chromatography DEAE-Cellulose Microbiology Sucrase Animals Trehalase Ascaris suum Swine Diseases Ascariasis Ascaris General Medicine Hydrogen-Ion Concentration biology.organism_classification Disaccharidase Intestines Infectious Diseases Invertase Solubility Biochemistry Female Parasitology Maltase Glucosidases |
| Zdroj: | Experimental Parasitology. 35:125-131 |
| ISSN: | 0014-4894 |
| DOI: | 10.1016/0014-4894(74)90015-0 |
| Popis: | Disaccharidases from the gut of Ascaris suum were investigated to determine whether they were synthesized by the worm or whether they were host enzymes adsorbed to the worms' intestinal cells. Alpha-d-glucoside glucohydrolase (maltase) (EC 3.2.1.20), Beta-d-fructofuranoside fructohydrolase (invertase) (EC 3.2.1.26) and 1-glucohydrolase (trehalase) (EC 3.2.1.28) from Ascaris were studied in both a membrane (brush border)-bound and solubilized form with regard to temperature stability and pH optima. Data collected were compared to similar data on hog intestinal enzymes. Worm maltase and trehalase were relatively heat labile, whereas the hog enzymes were more stable to heat inactivation. Worm invertase was heat stable in comparison to the hog enzyme. The pH optima for Ascaris maltase and invertase were different from those of hog disaccharidases, whereas the pH optimum for trehalase from both parasite and host were similar. Tissue homogenates of second-stage larvae contained measurable maltase, but not sucrase, or trehalase activity. Results suggested that Ascaris intestinal disaccharidases represent three distinct enzymes of parasite rather than host origin. |
| Databáze: | OpenAIRE |
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