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

A multi-lumen intubation system was used to study the absorption of calcium, glucose and galactose in 13 human subjects. The intubation was placed between the duodenum abdomen and proximal jejunum and the subjects were perfused with milk and lactase-supplemented milk. Lactose disappearance over a 20 cm length of intestine was used as the index of lactase activity. The subjects were assigned to one of two groups, lactase-normal and lactase-deficient. There was linear correlation between the absorption of calcium and lactose: lactase-deficient subjects absorbed less calcium than lactase-normal subjects. Perfusion with lactase-supplemented milk enhanced calcium absorption in lactase-deficient subjects but had no effect on that of normal lactase subjects. All subjects absorbed approximately the same percentage of perfused calcium (24%) when perfused with hydrolysed milk. These data indicate that the enhancement of calcium absorption is not a function of lactase per se, but of its hydrolytic products, glucose and galactose.
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PMID:Effect of lactose hydrolysis on calcium absorption during duodenal milk perfusion. 314 89

The disaccharide lactose, the principal carbohydrate of animal milks, requires the enzyme lactase to split it to glucose and galactose. Undigested lactose passes to the colon where fermentation produces hydrogen and short-chain fatty acids that can cause abdominal distention, pain and sometimes diarrhea. Persistence of intestinal lactase after early childhood, is inherited as a highly-penetrant autosomal dominant genetic characteristic. On the basis of a review of over 560 references, all available data on the primary loss of intestinal lactase in Latin American populations are presented in tabular form. Prevalence of lactose non-digesters in Latin American populations ranges from 45% to 100%. However, this is not a reliable predictor of the acceptability of milk and milk products containing lactose. Milk is being used successfully for the supplementary feeding of children worldwide, and most lactose non-digesters can tolerate at least 240 ml of milk or the lactose equivalent in other products. Lactose maldigestion does not interfere with the absorption of the protein and essential micronutrients in milk. Information is provided on the lactose content of milk and milk products, on the usual milk consumption of Latin American populations, and on worldwide experimental and field observations of milk acceptability. Both adaptation to continued use of milk and milk products and relationships of milk use to various disease states in which intestinal lactase activity may be reduced are discussed. Some types of yoghurts are better tolerated because of the lactase activity of the bacteria used in their fermentation. For unusually intolerant individuals commercial enzyme preparations are available for addition to milk products but for most persons the additional cost is unnecessary.
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PMID:[Lactose tolerance and milk consumption: myths and realities]. 315 50

The relationship between primary lactase deficiency, the amount of lactose in the diet, and symptoms of intolerance continues to be debated. Primary adult lactase deficiency is common with a worldwide occurrence of near 70%. Lactase-deficient individuals malabsorb lactose but may or may not show intolerance symptoms. The development of symptoms appears to depend on the dose of lactose ingested, whether it is accompanied by a meal or other food, rate of gastric emptying, and small intestine transit time. Lactose loads of 15 g or greater produce symptoms in the majority of lactase-deficient persons. However, when lactose loads of up to 12 g are fed, symptoms can be minimal or absent. Tolerance to yogurt, acidophilus milk, and other microbe-containing dairy foods has been suggested and is thought to be due to either a low lactose content or in vivo autodigestion by microbial beta-galactosidase. Up to 20 g of lactose in yogurt is tolerated well by lactase-deficient persons. Associated with the consumption of yogurt is a three- to fourfold reduction in lactose malabsorption as compared with similar lactose consumption in milk. Improved lactose digestion appears due to autodigestion by microbial beta-galactosidase. This enzyme may be released from yogurt culture by gastric or bile acid digestion. Feeding yogurt that was pasteurized following fermentation, with only trace amounts of microbial beta-galactosidase activity, results in a threefold increase in lactose malabsorption as compared with feeding yogurt with a viable culture. However, pasteurized yogurt also is tolerated well by lactase-deficient persons, suggesting that tolerance of up to 20 g of lactose in yogurt may be independent of lactose malabsorption. The enhanced lactose absorption and tolerance observed with yogurt feeding are not apparent when unfermented acidophilus milk or cultured milk are fed.
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PMID:Milk intolerance and microbe-containing dairy foods. 355 56

Protein, fat and carbohydrate absorption in preterm infants fed on human milk or formulae are reviewed. Even in the most premature infants absorption of protein is satisfactory. Nitrogen net absorption is about 85-90% of intake and results slightly lower with human milk than with formulae. The lower apparent digestibility of human milk is probably due to the poorly degraded IgA immunoglobulins and the rapid transit time. Lactose is well tolerated by the preterm infants despite the low lactase activity at birth. Glucose polymers, which have a low osmotic activity and are suitable for increasing carbohydrate intake of formulae, are well absorbed probably for the activity of salivary amylase and brush border glucoamylase, which have been shown to be well developed at birth. Premature infants absorb fat poorly. This malabsorption that increases with the lowering of gestational age is due to low pancreatic lipase activity and to low intraluminal concentration of bile salts. Due to its bile stimulated lipase activity, non-heat-treated human milk used at least in part is an effective method to improve fat absorption in preterm infants. Faecal energy determined using a calorimetric bomb appears to be a simple and an accurate method to predict faecal fat and avoiding expensive and cumbersome analysis.
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PMID:[Absorption of proteins, carbohydrates and fats in the preterm neonate]. 357 19

Considering 50 children affected by sub-acute gastrointestinal diseases by severe growth disorders, we have compared the "one-hour blood xylose test" with the "xylose and lactose H2 breath test, looking for a relationship with the duodeno-jejunal mucosal damage. Finally the integration between the "one hour blood xylose test" and the "xylose H2 breath test" may be useful in order to compare more exactly the results of both xylose tests with the mucosal damage. Lactose H2 breath test seems less reliable for our purposes because of the possible presence of children with lactase deficiences, hardly comparable with the mucosal damage.
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PMID:[Usefulness of the integration between the values of the 1-hour blood xylose test and the hydrogen breath-test after xylose oral load for the indirect evaluation of mucosa damage]. 409 11

Intolerance to lactose owing to deficiency of lactase is particularly prevalent among non-Caucasian peoples. Special caution is therefore needed in offering them milk supplements. Lactose tolerance has been investigated among the!Kung in the north-western Kalahari. The opportunity was taken also to examine their acetylator status, as this affects their ability to detoxicate drugs given for the treatment of tuberculosis and other diseases.The preliminary studies reported here suggest that not more than 10% of the!Kung are tolerant to lactose, but only one person out of 30 was a slow acetylator.
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PMID:Public health and genetic constitution of the San ("Bushmen"): carbohydrate metabolism and acetylator status of the Kung of Tsumkwe in the North-western Kalahari. 440 77

1. Three fractions of beta-galactosidase activity from the rat small-intestinal mucosa were separated chromatographically. Two of these fractions had an acid pH optimum at 3-4, and the third one had a more neutral pH optimum at 5.7. 2. The two ;acid' beta-galactosidase fractions had considerably lower K(m) values for hetero beta-galactosides than for lactose. The V(max.) values were similar for all the substrates used (lactose, phenyl beta-galactoside, o-nitrophenyl beta-galactoside, p-nitrophenyl beta-galactoside and 6-bromo-2-naphthyl beta-galactoside). No difference could be detected between the two ;acid' fractions with respect to their enzymic properties (pH optimum, K(m) for the different substrates, K(i) for lactose as an inhibitor of the hydrolysis of hetero beta-galactosides, K(i) for phenyl beta-galactoside as an inhibitor of the hydrolysis of lactose, and relative V(max.) for the hydrolysis of different substrates). These two fractions probably represent different forms of the same enzyme. 3. The ;neutral' fraction had similar K(m) values for all the substrates hydrolysed, but with lactose as substrate the V(max.) was much higher than with the hetero beta-galactosides. This fraction did not split phenyl beta-galactoside or 6-bromo-2-naphthyl beta-galactoside at a measurable rate. 4. Lactose was a competitive inhibitor of the hetero beta-galactosidase activities of all the three fractions, and K(i) for lactose as an inhibitor in each case was the same as K(m) for the lactase activity. Phenyl beta-galactoside was a competitive inhibitor of the lactase activity of all the three fractions. These facts strongly indicate that in all the three fractions lactose is hydrolysed by the same active sites as the hetero beta-galactosides. 5. Human serum albumin stabilized the separated enzymes against inactivation by freezing and thawing.
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PMID:Rat small-intestinal beta-galactosidases. Kinetic studies with three separated fractions. 572 84

1. Two beta-galactosidases from human small-intestinal mucosa were separated by gel-filtration chromatography and the properties of the two enzymes were studied. Lactose and four hetero beta-galactosides were used as substrates. 2. One of the enzymes was particle-bound and could be partially solubilized with papain. Of the substrates hydrolysed by this enzyme, lactose was hydrolysed most rapidly. This enzyme is thus essentially a disaccharidase and is named lactase. It is presumably identical with the ;lactase 1' described earlier. 3. The other enzyme was mainly soluble and hydrolysed all artificial substrates used, whereas no lactase activity could be detected. This enzyme has therefore been designated hetero beta-galactosidase. 4. p-Chloromercuribenzoate (0.1mm) inhibited the hetero beta-galactosidase completely but did not influence the activity of the lactase. Tris was a competitive inhibitor of both enzymes. 5. The residual lactase activity in the mucosa of lactose-intolerant patients may be exerted by a small amount of remaining lactase as such, or possibly by a third enzyme with a more acid pH optimum.
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PMID:Human small-intestinal beta-galactosidases. Separation and characterization of one lactase and one hetero beta-galactosidase. 582 67

Lactose tolerance tests with breath hydrogen determination identified 39 lactose malabsorbers among 162 Jordanian Bedouins (24%), and 111 lactose malabsorbers among 148 subjects from the urban/agricultural zone of western Jordan and Palestine (75%). This highly significant difference supports the hypothesis that milk dependence in nomadic desert populations resulted in selective pressures in favour of the lactase persistence gene. Within the urban/agricultural zone which extends from the desert border in Jordan to the Mediterranean shore, a significant increase in the frequency of lactose malabsorbers (and hypolactasia gene frequencies) from east to west was observed. The suggested genetic cline is problably due to migration from the desert populations to the agricultural zone.
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PMID:Distribution of adult lactase phenotypes in Bedouins and in urban and agricultural populations of Jordan. 641 7

Lactose absorption capacity was determined by lactose tolerance tests with breath hydrogen determination in 102 healthy, adult, Hungarian pairs of twins in order to test monogenic Mendelian inheritance of the absorptive lactase phenotypes, lactose absorber and lactose malabsorber. Of the total, 52 pairs were monozygous (MZ) and 50 dizygous (DZ) twins of identical sex. All MZ twins were concordant with respect to lactase phenotype. Among DZ twins, the distribution of lactase phenotypes was in agreement with Hardy-Weinberg expectations derived from the frequencies of the hypolactasia gene in DZ and MZ twins, and in the general Budapest population. In the second part of the study, three commonly used methods of lactose tolerance testing, the blood glucose, the blood galactose, and the breath hydrogen tests, were compared in 49 pairs of twins concordant for lactase phenotype. Blood galactose concentration showed the greatest and only significant difference between the intrapair correlation coefficients of MZ and DZ, and no overlap between lactose absorbers and lactose malabsorbers. The intrapair correlation coefficients of peak breath hydrogen concentration in MZ and DZ twins did not significantly differ from zero, but the resolution of lactase phenotypes was satisfactory. Differences in glucose absorption and concentration in lactose absorbers and malobsorbers overlapped considerably, and among lactose absorbers correlation coefficients in DZ were higher than in MZ twins. In MZ and DZ twins, the difference in concordance and constancy of lactose intolerance symptoms was not significant.
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PMID:A study of lactose absorption capacity in twins. 643 76


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