Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.2.1.23 (beta-galactosidase)
14,648 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The activities of the enterocyte brush border enzymes lactase (beta-D galactoside galactohydrolase, EC 3.2.1.23) and sucrase (sucrose alpha-D glucohydrolase, EC 3.2.1.48) were measured at set percentage lengths along the small intestines of 112 piglets killed between 21 and 32 days of age. The influences on these activities of consumption of creep feed and of weaning were recorded. Weaning at three weeks old resulted in large, rapid reductions in lactase activity at most sites along the small intestine; sucrase activity declined temporarily and then recovered. Minimum values were recorded about four to five days after weaning. Similar changes were observed whether or not creep feed was consumed before weaning. Continued consumption of creep feed by unweaned pigs over the 21 to 32 day period also produced small but significant reductions in lactase activities. The large loss of digestive enzyme activities at brush borders in weaned animals coincided with a reduced ability to absorb xylose and to checks in growth rate in otherwise healthy piglets.
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PMID:Influence of creep feeding and weaning on brush border enzyme activities in the piglet small intestine. 308 80

Hydrocortisone administration to infant rats enhanced cellobiase and maltase activities and induced precocious expression of sucrase and trehalase activities along the length of the small intestine. These activity changes reflected proportional concentration increases in the enzymes lactase (EC 3.2.1.23), maltase/glucoamylase (EC 3.2.1.20) and sucrase-isomaltase (EC 3.2.1.48/10). Administration of an equivalent tracer dose of [3H]leucine (by body weight) to control and hydrocortisone-treated infant rats resulted in greater accumulation of label in the carbohydrase pools of the treated rats, suggesting their increased de novo synthesis. The increased concentrations of lactase and maltase/glucoamylase induced by exogenous hydrocortisone were matched by the presence of corresponding greater amounts of label in their brush border pools. Accumulation of label in each of the lactase, maltase/glucoamylase and sucrase-isomaltase pools was generally similar in the hydrocortisone-treated rats, suggesting equivalent stimulation of their synthesis as a group by the humoral agent. The turnover rates of the carbohydrases as a group were found to be similar and did not appear to differ in control and hydrocortisone-treated rats. Total protein synthesis rates were slightly greater in the intestine of the hydrocortisone-treated group of rats.
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PMID:Effects of hydrocortisone on carbohydrase concentrations, de novo synthesis and turnover patterns in immature rat intestine. 308 73

The effect of streptozotocin (SZ) on the development of small intestinal enzymes in postnatal rat pups was studied. SZ was injected ip on Day 10 and, if necessary, again on Day 12. On Days 15, 18, and 21, one pup from each group (including a vehicle-injected control (C) group) was decapitated under conditions which minimized stress. Plasma glucose, insulin (IRI), and corticosterone were measured, as were pancreatic IRI, liver glycogen, and liver membrane binding of IRI. Small intestinal segments were processed and analyzed for sucrase, lactase, maltase, and ileal acid beta-galactosidase activities. Our results indicate that plasma glucocorticoid levels remained virtually constant in both SZ and C groups, while the ontogenic profiles of sucrase and maltase in SZ rats were shifted toward an earlier appearance and a precocious maturation. Circulating levels of IRI were not reduced significantly by SZ despite the fact that pancreatic IRI was decreased 95%. Jejunal lactase, unlike data reported for diabetic rats, was not affected by SZ diabetes. Also, acid beta-galactosidase was unaltered in the SZ rat pups. It is concluded that possibly the elevated disaccharidases seen in diabetic postnatal rat pups are the direct effect of elevated blood glucose. If so, the SZ rat pup model may be a useful tool with which to study effects of glucose on intestinal enzymes in the absence of changes in plasma insulin.
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PMID:Effects of diabetes on development of small intestinal enzymes of infant rats. 312 20

Studies of intestinal enzyme development and regulation relevant to the human infant require an animal model with a rate of maturation similar to that of the human infant. Hanford miniature pigs were weaned at 3 days of age to a standard swine weaning formula. At 1, 2, 3, 4, 5, and 6 wk of age, duodenal jejunal, and ileal segments were analyzed for protein content and lactase, sucrase, maltase, glucoamylase, and acid beta-galactosidase activities. Protein content of the small intestine changed significantly with age only in the ileum (p less than 0.05). Lactase activity fell significantly with age in all segments of the small intestine (p less than 0.001); activity was highest in the jejunum. Sucrase and maltase activities were present in all segments of the small intestine at 1 wk of age. Sucrase increased significantly (2-fold, p less than 0.02) with age only in the ileum and maltase increased significantly with age in the jejunum (by 50%, p less than 0.05) and the ileum (3-fold, p less than 0.001). Activities were highest in the jejunum. Glucoamylase activity was present at 1 wk of age and showed a small but significant increase with age only in the duodenum (p less than 0.005). Acid beta-galactosidase activity demonstrated small but significant decreases with age in all small intestinal segments. Glucoamylase and acid beta-galactosidase activities were similar in all segments. In the 6-wk-old pigs, activities of all the enzymes tested were similar to those found in young human infants.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:The miniature pig as an animal model for the study of intestinal enzyme development. 312 4

1. The intestinal disaccharidase activities of a suckling crabeater seal were investigated. 2. Lactase, maltase, isomaltase and cellobiase activities were readily detected but trehalase and sucrase activities were absent. 3. The intestinal homogenates were separated into a soluble (S2) fraction and a particulate brush border (P2) fraction. The lactase activities of the two fractions had different properties corresponding to those of an acid and a neutral beta-galactosidase respectively. Approximately two-thirds of the total lactase activity measured at pH 6.0 was due to the acid beta-galactosidase. 4. The isomaltase and cellobiase activities were found almost exclusively in the particulate fractions but about one third of the maltase activity was in the S2 fraction. This soluble maltase activity appeared to be due to an acid maltase.
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PMID:Intestinal lactase and other disaccharidase activities of a suckling crabeater seal (Lobodon carcinophagus). 313 70

1. Rats were fed on a control semi-synthetic diet containing insoluble cellulose (Solkafloc; 100 g/kg; control group) as the only source of dietary fibre, or on one of two test diets containing the same quantity of either guar gum or carboxymethylcellulose (CMC). Animals in the test groups showed similar growth rates and food intakes, which were significantly lower than those of the control group. The CMC group produced frequent poorly formed faeces throughout the 21 d feeding period. 2. The small intestines of animals in both test groups were significantly longer than those of the control group at the end of the study. The caeca were also enlarged and heavier, particularly in the CMC-fed group. 3. The rate of production of mucosal cells was increased in the small and large intestines of both test groups. The CMC-fed group exhibited a particularly high rate in the distal ileum, where the rate of cell divisions per crypt was over three times greater than at the same site in the control group. The increased proliferation was associated with a significant lengthening of the crypts and an approximately 25% increase in the basal width of the villi. 4. Mucosal alkaline phosphatase (EC 3.1.3.1) and lactase (EC 3.2.1.23) levels were lower than those of the control group at proximal and distal sites in the small intestines of both CMC- and guar-gum-fed groups. Altered spatial distributions of maltase (EC 3.2.1.20) and sucrase (EC 3.2.1.48) activities were also observed in these animals.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Gastrointestinal adaptation in response to soluble non-available polysaccharides in the rat. 367 72

We have examined the nature of the decline of lactase (EC 3.2.1.23) activity in the maturing rat intestine. It was established in an initial study that the activity decline reflected a proportional reduction in the concentration of the enzyme protein. Accumulation patterns of label into lactase, total intestinal proteins and sucrase (EC 3.2.1.48)-isomaltase (EC 3.2.1.10) were compared, 4 h following administration of a tracer dose of [3H]leucine to weanling rats exhibiting a wide range of lactase decline. Accumulation of increasing amounts of label in total intestinal proteins and sucrase-isomaltase pools was found to accompany the lactase decline, in contrast to accumulation of a constant amount of label in the declining lactase pools. The pattern of increased label accumulation in total intestinal proteins was shown in a corollary study to reflect a corresponding acceleration of total protein synthesis. On this basis, the finding of a constant amount of label in the declining lactase pools suggested a constant synthesis of lactase. We proposed earlier that associated reductions in enterocyte life-span (leading to correspondingly less lactase accumulation) rather than suppressed synthesis may provide the primary causal basis of lactase decline in the postweaned mammal.
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PMID:The nature of maturational decline of intestinal lactase activity. 392 28

The influence of two new 1-desoxynojirimycin derivatives, BAY m 1099 and BAY o 1248, on rat small intestinal disaccharidases (sucrase, maltase, isomaltase, glucoamylase, lactase, trehalase) and alkaline phosphatase activity has been investigated in vitro. Both compounds are very potent alpha-glucosidase inhibitors. Tested in the range of 0.1-5.0 micrograms/ml, inhibition is strongest on sucrase (up to 97.1%) and glucoamylase (up to 96.7%). BAY m 1099 also reduced (up to 56.4%) beta-galactosidase (lactase) activity. For both inhibitors a competitive type of sucrase inhibition was demonstrated (Lineweaver-Burk plot). Affinity versus sucrase was unusually tight. The Ki of BAY m 1099 versus sucrase amounted to 1.14 x 10(-7) M and of BAY o 1248 to 6.92 X 10(-8) M (Dixon plot). Both inhibitors did not impair active transport of L-leucine or methyl-alpha-D-glucoside into everted rings of rat jejunum in vitro.
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PMID:Effect of 1-desoxynojirimycin derivatives on small intestinal disaccharidase activities and on active transport in vitro. 403 92

Mucoid enteropathy was induced experimentally by ligation of the cecum, and the activities of mucosal disaccharidases and alkaline phosphatase were measured at different locations along the small intestine of the sick and control rabbits. In the duodenum of rabbits with mucoid enteropathy, the activity of acid beta-galactosidase II was elevated and hetero beta-galactosidase declined. In the jejunum, the activities of lactase, acid beta-galactosidase I and II, hetero beta-galactosidase, trehalase, sucrase and alkaline phosphatase were significantly lower in animals with mucoid enteropathy. In the ileum, acid beta-galactosidase II, hetero beta-galactosidase, maltase, trehalase, sucrase and alkaline phosphatase showed decreased activity in rabbits with mucoid enteropathy.
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PMID:Intestinal disaccharidase and alkaline phosphatase activities in experimental rabbit mucoid enteropathy. 409

The longitudinal distribution of different brush border enzymes along the human small intestine was studied by crossed immunoelectrophoresis. The results are based on biopsies taken every 50 cm in three intestines obtained at autopsy and on peroral or peroperative biopsies from the ligament of Treitz, proximal jejunum and distal ileum from 11 patients undergoing jejunoileal bypass operation for obesity. Lactase-phlorizin hydrolase (EC 3.2.1.23-62) and sucrase-isomaltase(EC 3.2.1.48-10) had their highest level in jejunum with decreasing activity towards the proximal and distal ends of the intestine, while maltase (EC 3.2.1.20) increased along the intestine and reached its highest activity in the distal ileum. A carboxypeptidase (EC 3.4.12.X) is demonstrated as an enzymatic entity of the human intestine. This enzyme had a rather flat distribution curve while microvillus aminopeptidase (EC 3.4.11.2), dipeptidyl peptidase IV (EC 3.4.14.X) and aspartate aminopeptidase (EC 3.4.11.7) all increased along the length axis and reached maximum values in distal ileum.
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PMID:Immunoelectrophoretic studies on human small intestinal brush border proteins--the longitudinal distribution of peptidases and disaccharidases. 611 68


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