Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.108 (lactase)
2,133 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Intestinal mucosa from 40 patients obtained by fiber-endoscopic biopsy was assayed for disaccharidases to determine suitability of this tissue for assay. The combined specimens from each patient provided 4.7-38.7 mg of tissue, adequate in all instances for duplicate determinations of protein, lactase, sucrase, and maltase. Tissue remained for assays of palatinase in 39 instances, trehalase and cellobiase in 37, and alkaline phosphatase in 22 cases. Twenty-four subjects had normal lactose tolerance tests and normal sucrase/lactase ratios. Thirteen patients with abnormal oral lactose tolerance tests were identified as having a primary low lactase activity on the basis of elevated sucrase/lactase ratios. This ratio was most helpful in making the diagnosis of a primary low lactase, since the mucosal specimens were not obtained from comparable areas. Tissue from three subjects with an abnormally low maltase was unsuitable for diagnosis. Endoscopic biopsy of mucosa appears to be satisfactory for disaccharidase assays in most instances.
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PMID:Adequacy of endoscopic biopsy specimens for disaccharidase assays. 10 20

Administration of D,L-thyroxine (T4) daily (25 or 250 nmol/100 g body weight/24 h) for 4 days increased jejunal activity in 15-day-old rats; no effect was seen in 8-day-old rats. Maltase activity was increased in 15-day-old rats only when a 250-nmol dose was used. Similar results were obtained in unoperated and adrenalectomized rats. Specific activity of lactase was not influenced in unoperated 8- and 15-day-old rats; it was decreased in adrenalectomized 8- and 15-day-old rats when treated with a 250-nmol dose of T4; in 15-day-old rats, it also responded to 25-nmol doses. The lowest dose used (2.5 nmol/100 g body weight) had no effect at all.
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PMID:Comparison of the effect of various doses of thyroxine on jejunal disaccharidases in intact and adrenalectomized rats during the first 3 weeks of life. 10 71

Intestinal lactase assays before and after a Billroth II procedure for chronic duodenal ulcer did not reveal a significant difference. Postoperative lactose intolerance is due to the loss of pyloric function, causing entrance of lactose into the jejunum at a rate exceeding the hydrolytic capacity of the mucosa if the lactase level is low.
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PMID:[Intestinal lactase and milk consumption before and after gastrectomy]. 10 82

The degree of which the ability to absorb lactose can be regained after recovery from an acute episode of severe malnutrition is in doubt. Lactase activity was indirectly assessed by means of a standard lactose tolerance test (2 g lactose per kilogram of body weight) in 71 Peruvian Mestizo infants and children (age 5 to 55 months) who had suffered such an episode. All were studied just before discharge after several months of hospital rehabilitation, during which linear growth and weight gain had accelerated and signs of significant malabsorption of other nutrients had disappeared. Only 39% of the total group had a positive test (delta blood glucose greater than 25 mg/dl); there was a decreasing proportion of positive responders with increasing age. No difference in response attributable to type or severity of malnutrition was found. Comparison of the present data with previous data from children in the same community who had never been acutely malnourished suggests that acute malnutrition may hasten the permanent decline of lactase activity normally expected later in life.
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PMID:Effect of an episode of severe malnutrition and age on lactose absorption by recovered infants and children. 10 90

A single injection of cortisone or thyroxine to 8-day-old suckling mice initiates a temporary decrease of lactase activity. On the contrary, 3 injections of cortisone or thyroxine provoke a significant increase of lactase activity. It appears that the mechanism which controls the postnatal development of lactase in suckling animals is more complex than expected.
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PMID:Opposite effects of one and three injections of cortisone or thyroxine on intestinal lactase activity in suckling mice. 10 33

At various postnatal stages, intestinal epithelial cells were isolated sequentially from villus tip to crypt base by successive EDTA treatments. According to the localization of marker enzymic activities, isolated cells were pooled into three cell compartments: villus (V), lower villus and upper crypt (VC) and crypt (C). Purified brush-border-membrane proteins were separated by 7.5%-polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. Enzymic activities could be assigned to some protein bands: maltase/glucoamylase (protein band 3), sucrase-isomaltase (protein bands 3 and 6), lactase (protein band 5) and alkaline phosphatase (region of protein bands 8 and 9). The findings suggest the following. (1) Sucrase-isomaltase activities appeared in compartment C at 17 days with a simultaneous increase of the pre-existing protein band 3 and appearance of a well-defined protein band in position 6; the enzymic complex remained still present in the crypt cells until adulthood. From the day 21 onwards, sucrase-isomaltase was detected in compartments VC and V. (2) Lactase was only present in the three cell compartments until day 21; at this developmental stage its activity completely disappeared from compartment C, in spite of the persistence of a weak protein band. (3) Alkaline phosphatase activity could be detected as a single peak corresponding to protein band 9 in all three cell compartments until day 21; thereafter it was replaced by two peaks of activity showing a less precise correlation with the well-defined protein bands 8 and 9. In the crypt cells of the adult rat, however, the preweaning situation, which was regularly observed, is an unexpected phenomenon. (4) Maltase and glucoamylase did not display any marked qualitative or quantitative modifications either along the villus-crypt axis or during the period of postnatal development studied. Evidence is given from the present data that each brush-border enzyme investigated has a specific developmental pattern.
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PMID:Developmental pattern of rat intestinal brush-border enzymic proteins along the villus--crypt axis. 10 86

General evidence of malnutrition such as loss in body weight associated with intestinal parasitism has been attributed to decreased food intake, to intestinal malabsorption, and to change in host basal metabolism. To establish the relative importance of these factors in this regard, rats with trichinosis were studied. The weights of infected and uninfected animals were followed after being placed on one of three feeding regimens for 1 week--stock diet ad libitum, intraduodenal nutrition, and intravenous nutrition. Infected rats on a stock diet lost weight whereas those on the other two regimens maintained the same weight pattern as uninfected counterparts. The maintainance of body weight occurred despite alterations at the level of the intestinal brush border as indicated by a depression of intestinal disaccharidase activities (sucrase and lactase) and by reduction of monosaccharide absorption (measured as accumulation of beta-methyl glucoside) in the proximal, heavily infected region of the small intestine. There was no compensatory increase in enzyme activity nor in the absorptive capacity in the distal gut. Results support the conclusion that inadequate oral food intake rather than changes in basal metabolism or intestinal pathophysiology accounts for weight loss during the intestinal phase of infection.
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PMID:Enteral and parenteral feeding to evaluate malabsorption in intestinal parasitism. 11 Jan 62

Lactase and maltase, the predominant sugar hydrolases associated with the intestinal brush bordermembrane of the suckling rat, were purified essentially free of the other to near homogeneity (lactase at specific activity 23, maltase at specific activity 58), and their specific physiocochemical properties determined. Antisera prepared to each showed by immunodiffusion a single common precipitin line with pure enzyme and solubilized proteins of the brush border membrane. Brush border membranes were purified 26--35-fold from infant rat intestine. Membranes prepared from 10-day-old rats contained 32% protein, 43% lipid and 25% carbohydrate with lactase and maltase estimated to comprise in excess of 10% and 2%, respectively, of the membrane protein. Immunotitration curves of lactase and maltase showed equivalent antibody binding by the membrane-bound and free enzyme forms. Furthermore, antibody binding to one enzyme did not affect the immunotitration curve or the extractability (by papain or Triton X-100) of the other membrane-bound enzyme. It was concluded that the lactase and maltase molecules are attached singly on the external membrane surface in a spatially independent manner with their antigenic sites as freely available to antibody binding as exhibited by their papain-solubilized counterparts.
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PMID:Sugar hydrolases of the infant rat intestine and their arrangement of the brush border membrane. 11 Mar 47

72 h after ligation or external fistulation of the common duct the activities of maltase, sucrase and lactase in the homogenate of the small intestinal mucosa of the rat were determined. The experiments were performed in connexion with intestinal perfusion studies, and the disaccharidase activities were measured in unperfused intestinal segments as well as in intestinal loops which had previously been perfused with a sucrose-containing solution. After bile duct ligation, the sucrase and maltase activities in a previously perfused intestinal loop were not different from those in sham-operated animals, the lactase activity was diminished. In a nonperfused segment, the sucrase activity was greater, the maltase activity was unchanged, and the lactase activity was lower than in control animals. After bile duct fistulation, the sucrase, maltase and lactase activities in a perfused segment were lower than in sham-operated rats. In a nonperfused loop, the sucrase activity was greater, the maltase activity was unchanged, and the lactase activity was lower then in the corresponding control group. These data suggest that bile is a factor which influences the total mucosal disaccharidase activities, and, probably, the intracellular enzyme distribution.
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PMID:Ligation or external fistulation of the common bile duct in the rat. II. Intestinal disaccharidase activities. 11 Jun 39

This study was undertaken to investigate the effect of alcohol on the activity of jejunal disaccharidases (DS). The activity of DS in a preparation of purified brush border membrane of hamster jejunum was measured in the absence and in the presence (0.8 to 6.4% wt/vol) of ethanol. To compare the effect of alcohol on DS with its action on a brush border enzyme of a different group, we also measured the activity of alkaline phosphatase (AP) under similar conditions. Ethanol depressed the activity of sucrase, maltase, and lactase in a dose-dependent and time-dependent manner, but it stimulated the activity of AP. The ethanol-induced inhibition of DS was completely reversible. Kinetic studies indicate that ethanol depressed the Vmax and increased the Km of sucrase and lactase. The Vmax of maltase also decreased, but the Km of this hydrolase was not affected by ethanol. From the results of this study it would appear that acute exposure of the jejunal brush border to ethanol depresses the DS activity of the membrane and that (because the AP was not depressed) the ethanol-induced inhibition of DS is not the result of a general inhibition of all enzymes of the brush border.
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PMID:Effect of ethanol on disaccharidases of hamster jejunal brush border membrane. 11 61


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