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)

A largely unrecognized immunoadsorbent desorption technique, hypotonic elution, has been successfully used in the immunoadsorbent purification of the microvillar enzymes aminopeptidase N (EC 3.4.11.2), dipeptidyl peptidase IV (EC 3.4.14.5), sucrase-isomaltase (EC 3.2.1.48-10), lactase-phlorizin hydrolase (EC 3.2.1.23-62) and maltase-glucoamylase (EC 3.2.1.20). This elution method proved capable of achieving an acceptable yield (30-70%) while at the same time preserving the purified enzymes in an enzymically active state. It hereby offers a solution to the problem in immunoadsorbent chromatography of finding an efficient means of elution which is not denaturing to neither the purified enzyme nor the immunoadsorbent column. Common properties of the microvillar enzymes with regard to amphiphilicity, glycosylation or subunit composition could hypothetically account for the similar elution properties of the enzymes but were considered unlikely on several grounds. Hypotonic elution in immunoadsorbent chromatography, therefore, may have a much broader range of applicability, and the method is recommended to be tried out by workers in other areas of protein chemistry.
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PMID:Hypotonic elution, a new desorption principle in immunoadsorbent chromatography. 612 6

Structural changes have been studied during the life cycles of three glycosidases: sucrase-isomaltase (EC 3.2.48-10), lactase-phlorizin hydrolase (EC 3.2.1.23-62), maltase-glucoamylase (EC 3.2.1.20); and three peptidases: aminopeptidase A (EC 3.4.11.7), aminopeptidase N (EC 3.4.11.2) and dipeptidyl peptidase IV (EC 3.4.14.5). The final forms of the enzymes can be divided into at least two groups: the sucrase-isomaltase type, characterized as dimers, which are asymmetric in their hydrophilic parts, have two types of active site and anchor only on one subunit; and the aminopeptidase N type, characterized as dimers, which are symmetric in their hydrophilic part, have only one type of active site and anchor on both subunits. These enzymes are likely to be synthesized on rough endoplasmic reticulum and simultaneously glycosylated into endoglycosidase H-sensitive forms. They are later reglycosylated to endoglycosidase H-resistant forms, which have relative molecular masses similar to the final forms. Enzymes of the sucrase-isomaltase type seem to be synthesized with a polypeptide-chain length corresponding to the sum of both subunits, whereas enzymes of the aminopeptidase N type seem to be synthesized with a polypeptide-chain length corresponding to the constituent subunits themselves. Not much is known about the catabolism of these enzymes. The enzyme activities and the amounts of enzyme protein decrease at the top of the villi, probably due to release into the lumen. The subunits of aminopeptidase N are cleaved by pancreatic proteases to smaller peptides, and sucrase-isomaltase may lose its sucrase polypeptide, while both enzymes remain bound to the membrane.
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PMID:Structure of microvillar enzymes in different phases of their life cycles. 613 6

Preparations of isolated brush border plasma membrane of Hymenolepis diminuta and H. microstoma possess the following enzymatic activities: alkaline phosphohydrolase (E.C. 3.1.3.1); Type I phosphodiesterase (E.E. 3.1.4.1); ribonuclease (E.C. 3.1.4.22); adenosine triphosphatase (E.C. 3.6.1.3); and 5'-nucleotidase (E.C. 3.1.3.5). The following enzymatic activities could not be demonstrated in either membrane preparation: Type II phosphodiesterase (E.C. 3.1.4.18); cyclic adenosine-3', 5'-monophosphate phosphodiesterase (E.C. 3.1.4.17); leucine aminopeptidase (E.C. 3.4.11.1); maltase (alpha-glucosidase; E.C. 3.2.1.20); and lactase (beta-galactosidase; E.C. 3.2.1.23). These data generally agree with those of previous studies in which similar membrane-bound enzymes were demonstrated in intact (living) worms.
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PMID:A comparison of membrane-bound enzymes of the isolated brush border plasma membranes of the cestodes of Hymenolepis diminuta and H. microstoma. 628 Jan 22

The active site-directed inhibitor 4-nitrophenyl-beta-D-galactopyranosylmethyltriazene, previously shown (Fowler, A. V., Zabin, I., Sinnott, M. L., and Smith, P. J. (1978) J. Biol. Chem. 253, 5283-5285) to alkylate methionine 502 in lacZ beta-galactosidase, was used to label the second naturally occurring beta-galactosidase of Escherichia coli (ebgo). The reagent was also used to label two mutant forms of the enzyme (ebga and ebgb) selected for enhanced lactase activity. In the case of ebgo and ebga, 75 and 85% of the label, respectively, was incorporated into a tryptic peptide which is homologous (38% identity) to residues 483-503 of the lacZ beta-galactosidase sequence. In the ebgo and ebga enzymes, a serine probably is alkylated. In the case of the ebgb enzyme, 61% of the label is found on a tryptic peptide homologous (69% identity) with residues 457-468 of the lacZ beta-galactosidase. In this peptide, a glutamic acid and a tyrosine residue are both alkylated.
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PMID:The active site regions of lacZ and ebg beta-galactosidases are homologous. 641 10

The beta-galactosidase activities of the rabbit small intestinal mucosa were studied over the pH range of 2.6 to 8.4, using different substrates, and in the presence or absence of the enzyme inhibitor p-chloromercuribenzoic acid. The results indicated the presence of 4 beta-galactosidases: (i) a neutral beta-galactosidase (lactase) with optimum pH of 5.8, (ii) an acid beta-galactosidase I with optimum pH of 3.4, (iii) an acid beta-galactosidase II with optimum pH of 4.6, and (iv) a hetero beta-galactosidase with pH optimum of 7.6. Seemingly, 3 of these beta-galactosidases were comparable with those in other mammals, and the 4th has not been reported in other species.
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PMID:Rabbit small intestinal beta-galactosidases. 642 19

Feeding yoghurt or base milk (from which the yoghurt was prepared by fermentation) to rats increased the counts of coliforms in the gut whereas the counts of lactobacilli were reduced by yoghurt but not by the base milk. Lactobacillus bulgaricus survived in the guts of gnotobiotic and conventional rats when yoghurt was fed continuously. Streptococcus thermophilus also survived in gnotobiotic rats but its ability to survive in conventional rats could not be examined. Both organisms failed to colonise the gut when a small inoculum of yoghurt was administered orally to germfree rats maintained on the stock diet. Streptococcus thermophilus but not Lact. bulgaricus grew in the rat diet when tested in vitro. Two enzyme systems (beta-galactosidase and lactase) were studied using, respectively, o-nitrophenyl-beta-D-galactopyranoside (ONPG) and lactose as the test substrates. Enzyme levels estimated with both substrates increased in the gut contents when rats were fed yoghurt but an increase was only found with ONPG in the intestinal mucosa fraction. The bacterial origin of all this increased activity is discussed. The other lactose-containing diets did not affect enzyme activity to the same degree. Feeding yoghurt changed the lactobacillus flora from one which was predominantly heterofermentative (Lact. reuteri ) to one which was predominantly homofermentative (Lact. salivarius).
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PMID:The effect of yoghurt on some components of the gut microflora and on the metabolism of lactose in the rat. 642 70

The biosynthesis of pig small intestinal lactase-phlorizin hydrolase (EC 3.2.1.23-62) was studied by labelling of organ cultured mucosal explants with [35S]methionine. The earliest detactable form of the enzyme was an intracellular, membrane-bound polypeptide of Mr 225 000, sensitive to endo H as judged by its increased electrophoretic mobility (Mr 210 000 after treatment). The labelling of this form decreased during a chase of 120 min and instead two polypeptides of Mr 245 000 and 160 000 occurred, which both barely had their electrophoretic mobility changed by treatment with endo H. The Mr 160 000 polypeptide is of the same size as the mature lactase-phlorizin hydrolase and was the only form expressed in the microvillar membrane. Together, these data are indicative of an intracellular proteolytic cleavage during transport. The presence of leupeptin during labelling prevented the appearance of the Mr 160 000 form but not that of the Mr 245 000 polypeptide, suggesting that the proteolytic cleavage takes place after trimming and complex glycosylation. The proteolytic cleavage was not essential for the transport since the precursor was expressed in the microvillar membrane in the presence of leupeptin.
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PMID:Biosynthesis of intestinal microvillar proteins. Intracellular processing of lactase-phlorizin hydrolase. 643 Feb 96

The addition of microbial beta-galactosidases directly to milk at mealtime represents a potential "enzyme replacement therapy" for primary lactase deficiency. We used the hydrogen breath test as the index of incomplete carbohydrate absorption to assess the efficacy of two enzymes--one from yeast, Kluyveromyces lactis (LactAid), and the other from the fungus Aspergillus niger (Lactase N)--to assist in the hydrolysis of 18 g of lactose in 360 ml (12 oz) of whole milk when consumed by an adult lactose malabsorber. Graded amounts of Lactase N produced, at best, a 53% relative reduction in breath hydrogen excretion, whereas quantitative elimination of excess hydrogen excretion was produced by 1 and 1.5 g of LactAid. A double-blind, controlled, crossover trial was subsequently performed in 50 healthy, unselected Mexican adults, to whom 360 ml of cow's milk was presented in the three forms in a randomized order: intact milk, prehydrolyzed milk, and milk to which 1 g of LactAid was added immediately before consumption. Among the 25 subjects with incomplete carbohydrate absorption with intact milk, adding enzyme 5-min before consumption produced a 62% reduction in breath hydrogen excretion, and symptoms of intolerance were significantly reduced. The feasibility of effective enzyme replacement therapy with a beta-galactosidase from K. lactis is demonstrated.
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PMID:Enzyme replacement therapy for primary adult lactase deficiency. Effective reduction of lactose malabsorption and milk intolerance by direct addition of beta-galactosidase to milk at mealtime. 643 67

Comparisons between papain- and Triton X-100-solubilized lactase (EC 3.2.1.23) were made in terms of elution from various chromatographic columns and by molecular weight determinations. Using these techniques, no major differences could be detected. Since papain-solubilized enzyme would be cleaved at the hydrophilic-hydrophobic interface and detergent would release the amphipathic enzyme, the lack of detectable differences between purified lactase solubilized by the two agents suggests the existence of a relatively small anchoring moiety in rats when compared to that suggested in previous studies for adult humans.
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PMID:Comparison of detergent versus protease solubilized rat intestinal lactase. 643 55

The aim of this study was to determine the extent to which the postnatal maturation of intestinal hydrolases in the rat is dependent on the developmental rise of circulating corticosterone that occurs at the end of the 2nd wk of life. Pups were adrenalectomized (adX) on day 9 (i.e., before the developmental surge of corticosterone begins) and were killed on days 17, 20, 23, and 26. Serum corticosterone was measured to eliminate any incompletely adX animals. The rates of the developmental increases of sucrase and maltase activities and the developmental decreases of lactase and acid beta-galactosidase activities were depressed in adX pups aged 23 days and younger as compared with sham-operated controls. Administration of corticosterone (10 micrograms X g body wt-1 X day-1) to adX pups restored the developmental changes of these enzyme activities to rates equal to or greater than those in the sham-operated pups. By 26 days of age, all four enzyme activities of adX pups had reached their normal ontogenic plateau. We conclude that adrenal corticosteroids are potent determinants of the rate of developmental changes of intestinal hydrolases but that these hormones are not necessary for enzymes to eventually reach adult activities.
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PMID:Enzymic development of the small intestine: are glucocorticoids necessary? 674 20


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