Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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.
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PMID:Inhibition by selected food components of human and porcine intestinal pteroylpolyglutamate hydrolase activity. 229 33

Clinical differences between the two human intestinal mucosal folate conjugases were assessed by measurement of their activities in normal individuals and in patients with chronic diarrhea of differing causes. Intracellular folate conjugase (ICFC) was 15-fold more active than brush border folate conjugase (BBFC) in jejunal mucosa from seven obese patients undergoing elective gastric bypass surgery. The activity of ICFC was similar among normal volunteers and patients with diarrhea of unknown origin (DUO), gluten-sensitive enteropathy (GSE), inflammatory bowel disease (IBD), and the short bowel syndrome (IBD-SBS). By contrast, BBFC, sucrase, and lactase were decreased significantly in GSE, and BBFC was increased in IBD-SBS. The activity of BBFC correlated with lactase and with sucrase in the normal subjects and in patients with DUO, whereas no correlations were found with the activity of ICFC in any group. Our clinical studies confirm that ICFC and BBFC are different enzymes. ICFC is not affected by intestinal disease, whereas the activity of jejunal BBFC, like that of other brush border enzymes, is decreased by mucosal injury and is also capable of adapting to distal small intestinal disease or surgical resection.
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PMID:Clinical studies of intestinal folate conjugases. 308 71

During intestinal absorption, dietary polyglutamyl folates are hydrolyzed to monoglutamyl folates by pteroylpolyglutamate hydrolase (folate conjugase). This enzyme is present in the brush border and intracellular fractions of human jejunal mucosa. We compared the activities of brush border and intracellular folate conjugase (BBFC and ICFC), and other mucosal enzymes in the jejunum in continuity and bypassed loop in nine patients who underwent intestinal reconstitution operations 3 to 9 yr after jejunoileal bypass. Control jejunum was obtained from seven obese patients undergoing gastric bypass surgery. Jejunal morphometry showed mucosal hyperplasia with taller villi, larger crypts, and no change in cell size in the jejunum in continuity as compared to control or bypass jejunum. In brush border fractions, specific activities of sucrase and BBFC were significantly greater in the jejunum in continuity than in the control or bypass jejunum. In contrast, the specific activities of the other brush border and intracellular enzymes, including ICFC, were similar in all three segments. This is the first evidence that BBFC, like sucrase, adapts to luminal nutrition. The difference in response of BBFC and ICFC to diet and/or pancreato-biliary secretions provides evidence that these are distinct enzymes which are regulated by different mechanisms.
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PMID:Human intestinal folate conjugase: adaptation after jejunoileal bypass. 393 52

Absorption of labeled simple 3',5',9'-(3)H pteroylmonoglutamate, ([(3)H]PG-1) and conjugated pteroyl-mu[(14)C]glutamyl-gamma-hexaglutamate, ([(14)C]PG-7) folates was assessed in six patients with tropical sprue, before and after 6 mo of treatment, utilizing jejunal perfusion and urinary recovery techniques. Degradation products of [(14)C]PG-7 which were produced during perfusion were identified by DEAE-cellulose column chromatography. Jejunal mucosal activities of folate conjugase, lactase, sucrase, and maltase were measured in every patient. Malabsorption of both [(3)H]PG-1 and [(14)C]PG-7 was found in every untreated patient, with significant improvement after therapy. The urinary excretion of (3)H and (14)C paralleled the luminal disappearance of both isotopes. The chromatographic patterns of intraluminal degradation products of [(14)C]PG-7 obtained during perfusion did not differ from those previously found in normal subjects and were similar in studies performed before and after treatment. The activity of folate conjugase was increased in the mucosa of the untreated patients when compared to the post-treatment levels while the activities of mucosal lactase, sucrase, and maltase were originally low and increased significantly after therapy. These observations suggest that folate conjugase originates at a different mucosal locus than the brush border disaccharidases, and are consistent with previous evidence that folate conjugase is an intracellular enzyme. The present studies have demonstrated unequivocal malabsorption of both simple and conjugated folates in tropical sprue. In tropical sprue, folate malabsorption is the reflection of impaired folate transport and not of impaired hydrolysis.
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PMID:Jejunal perfusion of simple and conjugated folates in tropical sprue. 1669 65