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)

A study of the three-dimensional structure of the upper jejunal mucosa in diabetics has been carried out. The structural findings were related to 14C-L-phenylalanine uptake in vitro, sucrase activity in mucosal homogenates, and the enzyme content of the absorptive cells as measured cytophotometrically. A low grade mucosal transformation of the sprue-type was found, which was associated with decreased sucrase activity, and with no reduction in phenylalanine accumulation. On the other hand the specific activities of alkaline phosphatase, non-specific esterase, and succinic dehydrogenase in the surface cells remained unchanged.
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PMID:Quantitative study of mucosal structure, enzyme activities and phenylalanine accumulation in jejunal biopsies of patients with early and late onset diabetes. 52 68

During pregnancy and lactation in the rat the small intestine in general and the mucosal epithelium in particular gain weight. The specific activities of sucrase, lactate dehydrogenase and succinate-tetrazolium reductase remain constant and those of glucose 6-phosphate dehydrogenase and isocitrate dehydrogenase increase. There is no evidence that the reported decrease in absorption per unit area or weight of mucosal epithelium during pregnancy and lactation is due to decreases in enzyme activities within the epithelium. The pattern of enzyme change shows that the response of the gut to the stimuli of pregnancy and lactation must be a complex one, possibly involving increases in the specific activities of some enzymes.
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PMID:Adaptation of the small intestine during pregnancy and lactation in the rat. 53 27

The concomitant appearance of enterokinase (EK) and trypsin activities in the human intestinal mucosa is indicative of the importance of EK as an activator of trypsinogen and therefore as the key enzyme in protein digestion. Enterokinase can be detected in fetal mucosa from the 26th week of gestation on, paralleling appearance of tryptic activity in meconium. The developmental pattern of EK activity increases with age. Between 26 to 30 weeks of gestation, the EK activity is only 6% and full term babies (40 weeks) 20% of that found in older children. In contrast, lactase studies during development show a lactase activity of only 30% in human fetuses between 26 to 34 weeks of gestation as compared to full term babies. During the same gestational period, sucrase and maltase activities reach 70% of the full term. In addition, the distributional pattern of EK differs from the disaccharidases, showing the highest activity in duodenum and the lowest in ileum, whereas disaccharidases are highest in jejunum with lower activity in duodenum and ileum. Differences in topographical distribution and time of appearance of EK and disaccharidases may be attributed to differences in orgin as well as subcellular localization of these enzymes. It is conceivable that the premature infant, between 26 to 30 weeks of gestation, is better equipped to deal with hydrolysis of alpha-glucosides than of lactose.
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PMID:Developmental pattern of small intestinal enterokinase and disaccharidase activities in the human fetus. 55 25

The effect of cows' milk protein (CMP) on the mucosal disaccharidases was investigated in 23 infants with acute infective enteritis. Jejunal biopsies performed before and after cows' milk provocation were subjected to histological examination and to mucosal disaccharidase enzyme (lactase, sucrase, and maltase) analyses. After milk challenge, changes in mucosal histology were observed in 18 infants, in 17 of them the levels of all 3 mucosal disaccharidases were much reduced. 10 of these infants developed diarrhoea and, in 6, the stools were positive for reducing sugar. It is concluded that CMP has a deleterious effect on the jejunal mucosa of young infants recovering from infective enteritis, so that in the management of young infants with sugar intolerance secondary to infective enteritis, CMP and lactose should be excluded from the diet.
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PMID:Cows' milk protein-sensitive enteropathy: an important contributing cause of secondary sugar intolerance in young infants with acute infective enteritis. 57 Mar 76

The effect of graded (5, 10, 20, and 50%) chronic ethanol administration on the intestinal brush border enzymic activities has been investigated in the rat at three levels of the intestinal tract (duodenum, jejunum, ileum). Ethanol has been administered for 8, 15, 30, and 90 days. A 30% to 50% decrease of sucrase and alkaline phosphatase results, showing that the effect of alcohol appears in the first 8 days of intoxication is not reversible after 8 days of an alcohol-free diet. The effect of ethanol is not limited to disaccharidases. Impairment of alkaline phosphatase, peptidases and also enterokinases is observed. The decrease is more marked in the duodenum and jujunum than the ileum. The decrease of enzymic activity is generally maximal after 30 days of intoxication. There is then little further deterioration or even significant improvement. At the 30th day of ethanol administration, a clearcut dose-response relationship has been established. The results obtained suggest that ethanol exerts an effect on the intestinal mucosa which is not directly correlated to morphological villus changes.
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PMID:Intestinal brush border enzymes and chronic alcohol ingestion. 57 90

1. Specimens of human duodenal mucosa were obtained at duodenotomy. Superficial mucosal scrapings were homogenized in isotonic sucrose solution and fractionated by differential centrifugation. The distribution of organelles among the subcellular fractions was monitored by assay of suitable marker enzymes. 2. Enterokinase was recovered predominantly in the nuclear+brush-border fraction and 80% of the total activity was found to be particulate; approximately 20% of the enzyme was present in the soluble fraction, compared with 1% of the brush-border markers sucrase and alkaline phosphatase. 3. The brush-border-containing fraction was subfractionated by treatment with hypertonic Tris followed by differential and density gradient centrifugation. Enterokinase was distributed among the subfractions in parallel with brush-border markers and was concentrated in a subfraction which was highly enriched in microvillous membranes. 4. It was concluded that enterokinase is localized primarily to the microvillous membrane of the epithelial cell brush border in man, but that in addition a proportion of the enzyme may be present in a soluble or easily released form in the duodenal mucosa.
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PMID:Subcellular localization of enterokinase in human duodenal mucosa. 58 40

Camels with cannulas in the small intestine were used to study the "digestive-absorptive" capacities of the small intestine. Solutions of different carbohydrates were infused through the cannulas and the responses in blood glucose levels were measured. Monosaccharides were readily absorbed from the camel small intestine. The pattern of disaccharide absorption indicated that there was high lactase activity and low maltase and sucrase activity, in the camel small intestinal mucosa.
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PMID:Studies on the digestion of carbohydrates in the camel (Camelus dromedarius). 59 40

The authors review the contemporary uses of histochemistry for the diagnosis of enzymopathies. Enterokinase, lactase, sucrase and trehalase deficiency can be diagnosed by histochemical methods. In glycogenoses, glycogen storage and glucose-6-phosphatase, acid alpha-glucosidase and phosphorylase deficiencies can be demonstrated. In mucopolysaccharidoses, the accumulation of acid muco-substances and changes in lysosomal enzyme activities can be demonstrated.
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PMID:Possibilities for the cytochemical diagnosis of enzymopathies. 61 85

7 infants, aged 5 weeks to 11 months, with clinically documented intolerance to cow's milk protein, chronic diarrhea, and failure to thrive, underwent small intestinal (peroal, suction) biopsy before and after withdrawal of milk proteins. Mucosal specimens were examined by light microscopy and assayed for disaccharidase activities. In all patients, moderate to severe mucosal changes were presented, associated with marked inflammation of lamina propria and damages to the brushborder. Disaccharidase activities (lactase, sucrase, maltase and palatinase) were markedly depressed in all. Follow-up biopsies were obtained in 6 infants, after 3-5 months on a milk-protein-free diet. At the time of the second biopsy, the disaccharidase activities had risen significantly and histologic improvement had occurred in each instance. In infancy, intestinal mucosal lesions due to intolerance to cow's milk protein are histologically indistinguishable from those seen in gluten-sensitive enteropathy and are associated with marked secondary disaccharidase deficiencies. Following therapy, the activity of the disaccharidases become normal or near normal prior to the complete morphologic recovery of the small intestinal mucosa.
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PMID:Disaccharidase deficiency in infants with cow's milk protein intolerance. Response to treatment. 62 28

Sucrose catabolism was studied in Rhodopseudomonas capsulata. Sucrose was hydrolysed by the action of a constitutive cytoplasmic sucrase. The use of a glucose-6-phosphate dehydrogenase-deficient mutant and radiorespirometric experiments demonstrated that both the glucose and fructose moieties of sucrose were catabolized via the Entner-Doudoroff pathway. This result was confirmed by enzyme analysis and studies on sugar assimilation. All the enzymes of the Entner-Doudoroff pathway were present in bacteria grown on secrose but fructokinase (EC 1.7.1.4) activity was relatively low. In contrast, phosphoenolpyruvate:fructose phosphotransferase and 1-phosphofructokinase, the key enzymes for the catabolism of exogenous fructose, were only partially induced. Bacteria grown on sucrose and treated with chloramphenicol were, therefore, not able to assimilate exogenous fructose. We conclude that under these conditions endogenous fructose is catabolized via the Entner-Douboroff pathway, while exogenous fructose is degraded via fructose 1-phosphate and the Embden-Meyerhof pathway.
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PMID:An alternative pathway for the degradation of endogenous fructose during the catabolism of sucrose in Rhodopseudomonas capsulata. 64 27


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