Demonstration of sucrase-isomaltase complex in chick intestine.
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Abstract:
It was investigated whether sucrase and isomaltase form an enzyme-enzyme complex in chick intestine or not, and some properties of the disaccharidases were compared with those of other species. 1) Chick intestinal sucrase and isomaltase were shown to exist in the form of an enzyme-enzyme complex from the results of polyacrylamide disc gel electrophoresis, DEAE Sephadex A-25 ion exchange column chromatography and citraconylation, although the chick intestinal sucrase and isomaltase were not retained on a Sephadex G-200 column. 2) The molecular weights of sucrase-isomaltase complex, maltase I, maltase II, maltase III and isomaltase dissociated from sucrase-isomaltase complex were estimated to be 250,000, 250,000, 160,000, 225,000 and 80,000, respectively, by polyacrylamide disc gel electrophoresis. 3) The optimum pH for all the enzymes was 6.0. 4) Km values of sucrase, isomaltase, maltase I and maltase III were 10.0, 3.5, 1.0 and 4.6 mM, respectively. Vmax values for sucrase, isomaltase, maltase I and maltase III were 217.4, 281.4, 147.1 and 454.5 mumol substrate hydrolyzed/mg protein/hr, respectively.Keywords:
Sucrase
Maltase
Sephadex
Disaccharidase
Lactase
The intestinal brush border disaccharidases separated by gel electrophoresis were studied after oral administration of a high sucrose or lactose diet to 11-day-old suckling rats during 3 days. Some modifications of the brush border protein and eyzyme patterns could be attributed to the effect of the basic diet: increase of glucoamylase, appearance of a weak sucrase activity and of a second molecular form of maltase. However, the specific action of a given disaccharide on the synthesis of the corresponding hydrolytic enzyme could be clearly demonstrated. Indeed, the electrophoretic pattern after sucrose or lactose feeding showed a marked increase of the protein bands corresponding to sucrase-isomaltase or lactase activities.
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The disaccharides, consisting of sucrose, lactose and maltose, are hydrolysed into monosaccharides (D-glucose, D-galactose and D-fructose) by intestinal brush border enzymes: sucrase, lactase and maltase. The aim of this study to investigate changes in the brush-border membrane carbohydrate digestive enzymes. From intestinal mucosal scrapings of equine, brush border membrane vesicles were isolated. The results showed that sucrase, maltase and lactase are present in the equine small intestine. The activity of all three enzymes is highest proximally (in the duodenum and jejunum) and lower in the ileum. There was considerable variation between individual horses, however the majority showed highest disaccharidase activity in the jejunum, with some showing highest activity in the duodenum. Sucrase activity is highest in the jejunum and duodenum and lower in the ileum. Maltase activity is similar in all three regions, but slightly higher in the jejunum. Lactase activity is low in all three regions of the small intestine, slightly higher in the equine jejunum and duodenum than ileum. From this study, we can conclude that the equine small intestine digests disaccharides by the brush-border associated disaccharidases sucrase, maltase and lactase. Levels of sucrase and lactase are comparable to other species, but maltase is much higher.
Disaccharidase
Sucrase
Maltase
Lactase
Jejunum
Brush border
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Brush border enzymatic activities (maltase, lactase and sucrase) have been determined in the ileal mucosa of rats subjected to a 30% ethanol ingestion for 3 and 5 months. The data were compared with the results obtained with control rats. Mucosal protein content after 3 months of ethanol treatment was similar to that of control rats. Maltase, lactase and sucrase specific activities in ileal mucosa were significantly decreased in ethanol-fed animals as compared to control rats. After 5 months of ethanol consumption, the protein content was decreased in ethanol-fed rats. However, no differences were found between specific activities of maltase, lactase and sucrase of ethanol-fed with respect to control rats. It is suggested that prolonged exposure of rats to ethanol results in adaptive responses to the effects of shorter periods of exposure on intestinal mucosal function.
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Gudmand-Höyer, E., Asp, N.-G. & Möllmann, K.-M. Disaccharidase activi-ties in intestinal metaplasia - contribution of lysosomal and brush border enzymes. Scand. J. Gastroent. 1975, 10, 653-656.Maltase, sucrase, and lactase were measured at pH 4 and pH 6 in normal and intestinalized gastric mucosa. In the normal mucosa the low activities of maltase and lactase seemed to be entirely due to lysosomal enzymes with acid pH-optimum. In intestinal metaplasia, brush border maltase and sucrase, but not lactase, appeared. On the other hand, there was a significant increase in lysosomal lactase (ß-galactosidase) activity.
Disaccharidase
Sucrase
Maltase
Lactase
Brush border
Intestinal metaplasia
Alpha-glucosidase
Intestinal mucosa
Metaplasia
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1. Maltase sucrase, palatinase (the enzyme that hydrolyses palatinose, i.e. 6-o-α-D-gluco-pyranosyl-D-fructose) and lactase activities were measured in the small and large intestines of germ-free and conventional chicks given either a diet of purified ingredients or a practical chick mash. 2. With the purified diet there were no differences in body-weight or small intestinal disaccharidase activities between germ-free and conventional chicks. With the chick mash the germ-free birds were heavier and had higher total amounts of maltase, sucrase and palatinase activities in the small intestine than did their conventional controls. When disaccharidase activities were expressed in terms of body-weight there were no differences between birds in the two environments. Enzyme activities were consistently higher in the birds given chick mash. 3. Inclusion of milled fibre in the purified diet did not increase the weight or disaccharidase activities of the small intestine in either environment. 4. Lactase was virtually absent from the small intestine of birds in both environments and from the large intestine of germ-free birds. There was appreciable lactase activity in the large intestinal contents of conventional chicks, and it was increased by inclusion of lactose in the diet. 5. When lactose was the sole source of carbohydrate the birds grew poorly but mortality rate was less among conventional compared with germ-free chicks. 6. It was concluded that the presence of micro-organisms has no direct effect on disaccharidase production in the small intestine of the chick. Microbial lactase is present in the large intestine, and at least some of the products of its action can be utilized by the bird.
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Disaccharidase
Maltase
Sucrase
Lactase
Hindgut
In ovo
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Disaccharidase activities in intestinal metaplasia - contribution of lysosomal brush border enzymes.
Maltase, sucrase, and lactase were measured at pH 4 and pH 6 in normal and intestinalized gastric mucosa. In the normal mucosa the low activities of maltase and lactase seemed to be entirely due to lysosomal enzymes with acid pH-optimum. In intestinal metaplasia, brush border maltase and sucrase, but not lactase, appeared. On the other hand, there was a significant increase in lysosomal lactase (beta-galactosidase) activity.
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Maltase
Lactase
Brush border
Intestinal metaplasia
Alpha-glucosidase
Intestinal mucosa
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The objective of this study was to determine and describe the age-related changes in intestinal brush border membrane enzyme activities that occur in C57Bl/6 mice. Specifically, jejunal, duodenal, and ileal dipeptidyl peptidase IV/CD26, disaccharidase (lactase, sucrase, and maltase), and alkaline phosphatase activities were determined. A significant correlation between analyzed intestinal brush border membrane enzyme activities and animal age was found. Our study revealed that intestinal dipeptidyl peptidase IV/CD26, lactase, sucrase, maltase, and alkaline phosphatase activities decline significantly with age (p < .05). Nevertheless, the horizontal (duodenum to ileum) enzyme activity patterns are not affected by age.
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Maltase
Lactase
Dipeptidyl peptidase
Brush border
Alpha-glucosidase
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Digestive enzymatic activities (maltase, lactase and sucrase) have been determined in the intestinal mucosa of rats subjected to a jejunoileal bypass of 45 cm. The weight and protein content of the mucosa (mg/cm) were significantly decreased in the bypassed segment and significantly increased in the unbypassed segment, as compared to control rats. Maltase, lactase and sucrase specific (U/g protein) and total activity (U/cm intestine) were significantly decreased in the bypassed jejunum, compared to sham-operated rats. In the ileum, maltase specific and total activities increased in bypassed animals while the lactase and sucrase activities remained unchanged.
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Sucrase
Lactase
Maltase
Jejunum
Jejunoileal bypass
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Disaccharidase
Maltase
Sucrase
Brush border
Lactase
Jejunum
Alpha-glucosidase
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Citations (31)