Inhibition by selected food components of human and porcine intestinal pteroylpolyglutamate hydrolase activity
| Autor: | Jesse F. Gregory, Sneh D. Bhandari |
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| Rok vydání: | 1990 |
| Předmět: |
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Swine Biological Availability Medicine (miscellaneous) Cysteine Proteinase Inhibitors In Vitro Techniques Biology Intestinal absorption Sucrase medicine Animals Humans Intestinal Mucosa Orange juice Plants Medicinal Nutrition and Dietetics Microvilli Plant Extracts food and beverages Fabaceae gamma-Glutamyl Hydrolase Trypsin Diet Bioavailability Intestines Pteroylpolyglutamic Acids Intestinal Absorption Biochemistry Fruit Alkaline phosphatase Gamma-glutamyl hydrolase medicine.drug |
| Zdroj: | The American Journal of Clinical Nutrition. 51:87-94 |
| ISSN: | 0002-9165 |
| Popis: | Studies were conducted to determine the in vitro effect of selected food components on activity of the brush border membrane pteroylpolyglutamate hydrolase (folate conjugase) of porcine and human intestine. Foods differed widely in their effects although the pattern of the effects on both porcine and human enzymes was similar. Extracts of legumes, tomatoes, and orange juice consistently inhibited the conjugase activity. Citrate was also inhibitory to some extent. In contrast, extracts of cereal grain flours, whole egg, milk, cabbage, cauliflower, and lettuce caused little inhibition. Purified phytohemagglutinins, soybean trypsin inhibitors, and bovine milk folate-binding protein had no effect on the conjugase activity at the concentrations tested. The food substances that inhibited the conjugase activity did not bind the polyglutamyl folate substrate or inhibit intestinal brush border membrane sucrase and alkaline phosphatase. These findings suggest that food composition may influence folate bioavailability by interfering with the intestinal deconjugation of dietary polyglutamyl folates. |
| Databáze: | OpenAIRE |
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