Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.1 (alkaline phosphatase)
 47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The pH of optimum activity of alkaline phosphatase from cow's milk depended on the substrate, being 10-1 for rho-nitrophenylphosphate, 8-6 for phosphoserine, 8-0 for phosvitin and 6-8 for casein. Individual casein components were dephosphorylated more rapidly than mixtures of alphas- and beta-caseins or of alphas-, beta-and kappa-caseins and micellar casein. Mixtures of 2 components involving kappa-casein were more readily dephosphorylated than alphas- and beta-casein mixtures. At pH 6-8, lactose, whey proteins and phosphate ions had an inhibitory effect. beta-Lactoglobulin had an inhibitory effect only when the pH of the reaction was lower than the optimum pH value of the enzyme. Mg2+ and Zn2+ were not inhibitory. The optimum conditions for dephosphorylation of casein are described.
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PMID:Dephosphorylation of bovine casein by milk alkaline phosphatase. 0 76

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

The mechanisms for transport and hydrolysis of lactose were investigated in five cariogenic strains (HS6, AHT, FA1, NCTC 10449, and SL1) representing the four serogenetic groups of Streptococcus mutans. The systems for transport and hydrolysis of lactose had the characteristics of a phosphoenolpyruvate (PEP)-dependent lactose (Lac) phosphotransferase (PT) system and phospho-beta-galactosidase (P-beta-gal), respectively, in all strains tested, except strain HS6. Decryptified cells required PEP and Mg(2+) for transport of the non-metabolizable model beta-galactosides o-nitrophenyl-beta-d-galactopyranoside (ONPG) and thiomethyl-beta-d-galactopyranoside (TMG). Substitution of 2-phosphoglycerate (2-PG) for PEP also stimulated the Lac PT system. Other potential high-energy phosphate donors (adenosine tri-, di-, and monophosphates and guanosine triphosphate) did not stimulate the Lac PT system. Sodium fluoride had no effect upon the PEP-dependent Lac PT system in decryptified cells with PEP as the energy source; however, when 2-PG was used as the energy source, F(-) inhibited ONPG phosphorylation. With intact cells which must generate PEP endogenously, the presence of F(-) in concentration >/= 10 mM completely inhibited the Lac PT system, presumably through inhibition of 2-PG hydrolyase (EC 4.2.1.11; enolase). Both intact and decryptified cells accumulated a phosphorylated derivative of TMG that behaved chromatographically as TMG-phosphate. After alkaline phosphatase treatment, the derivative had an R(f) identical to that of TMG. No beta-galactosidase (beta-gal) activity was detected with ONPG as the substrate; hydrolysis occurred only when ONPG-6-phosphate was supplied as the substrate. Strain HS6 apparently transported lactose by an active transport-type system in which the accumulated intracellular product was the free disaccharide based on the following criteria: (i) ONPG transport and hydrolysis in decryptified cells was not stimulated by PEP; (ii) ONPG hydrolysis occurred in the absence of PEP; and (iii) ONPG-6-phosphate was not hydrolyzed. These data indicate that, in all strains tested except strain HS6, lactose transport was mediated by a PEP-dependent Lac PT system, resulting in accumulation of lactose-phosphate that was hydrolyzed by an enzyme similar to the P-beta-gal of group N streptococci and Staphylococcus aureus; conversely, strain HS6 transported and hydrolyzed lactose by a PEP-independent transport system and beta-gal, respectively.
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PMID:Involvement of phosphoenolpyruvate in the catabolism of caries-conducive disaccharides by Streptococcus mutans: lactose transport. 24 29

The receptor specificity of the plant seed toxin ricin, which ordinarily binds to galactose-containing receptors, has been altered by coupling monophosphopentamannose residues to ricin by reductive amination and by reversibly binding lactose to the modified ricin. The added monophosphopentamannose residues provide ricin with the recognition factor common to fibroblast lysosomal hydrolases and enable the modified ricin (Man6P-ricin) to bind to the fibroblast Man6P receptor and inhibit protein synthesis in the cells via this receptor. The addition of lactose to Man6P-ricin saturates the galactose site on Man6P-ricin and prevents the binding of Man6P-ricin to cells via galactose-containing ricin receptors. The Man6P receptor-mediated toxicity of Man6P-ricin, identified in human fibroblasts by competition by Man6P and blockade by alkaline phosphatase treatment, was not detected in HeLa cells or human amnion cells. Consequently, in the presence of lactose, the fibroblasts were 8 and 13 times more sensitive than amnion and HeLa cells, respectively. These results show that highly toxic cell-type-specific reagents can be made by the proper alteration of toxin receptor specificities. An attempt to construct a highly toxic altered toxin by adding Man6P residues to diphtheria toxin fragment A was unsuccessful. A possible explanation is that in Man6P-ricin the ricin B chain performs some entry function, even though the initial binding step occurs at the Man6P receptor.
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PMID:Ricin linked to monophosphopentamannose binds to fibroblast lysosomal hydrolase receptors, resulting in a cell-type-specific toxin. 29 62

The effects of carbohydrate intake on jejunal disaccharidases in rats with chronic mannitol-induced, osmotic diarrhea were studied. Weanling rats were force-fed 5 ml/100 g of body weight of water of 20% mannitol (w/v 1300 mOsm) daily for up to 14 days. Diets containing 70% of either starch, sucrose, glucose, or 20% lactose with 50% starch were fed ad libitum. Mannitol-fed rats had increased water intake and diarrhea. They gained weight, but less than controls. The levels of intestinal disaccharidases in mannitol-fed rats were related to dietary carbohydrate intake. Seven days of mannitol treatment led to lactase and sucrase deficiencies in rats fed starch whereas jejunal maltase and alkaline phosphatase were unchanged. Deficiencies in lactase and maltase but not in sucrase were induced when rats were fed a sucrose diet, while a decrease only in sucrase occurred in rats fed a lactose-starch diet. Rats with mannitol-induced diarrhea fed a glucose diet had reduced levels of all disaccharidases. The changes in intestinal disaccharidases were not associated with alterations in the number of epithelial cells or ultrastructural abnormalities. 3H-thymidine incorporation into DNA following 7 days of mannitol treatment was similar to water-fed controls. Absorptive epithelial cells were not damaged and the microvilli were normal in height and appearance. These data suggest that the levels of specific disaccharidases show and enhanced dependence upon the corresponding dietary substrates during diarrhea induced by an osmotic load.
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PMID:Interaction between dietary carbohydrates and intestinal disaccharidases in experimental diarrhea. 85 Oct 74

Some biochemical and cytological investigations were carried out with milk and milk serum, blood and blood serum of 87 cows, of which 57 manifested symptoms of subclinical mastitis and 25 were normal. It was established that the milk of animals having subclinical mastitis had lower content of lactose, inorganic phosphorus, and sialic acids; on the other hand chlorides were at a higher level, and the activity of alkaline phosphatase rose. Besides, the contents of serum albumin and gamma-lactoglobulins showed dependable rise, while those of alpha-lactoglobulin and beta-lactoglobulin dropped. Dependable was likewise the drop of the total protein level. However, no changes were found in the total protein content and the distribution of protein fractions in the blood serum of cows manifesting inflammation of the udder.
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PMID:[Biochemical and cytological changes in the milk and blood of cows with subclinical mastitis]. 103 Aug 69

Lactase and cellobiase were detectable in the fetal intestine by the 3rd month of gestation, and although there was little change by the 9th month, maximal levels were reached at birth and steadily declined after 4 months. Conversely maltase, sucrase and trehalase were barely discernible in the fetus, maltase being present at low levels at birth, but all increased during the suckling period to attain adult levels by 7 months of age. Alkaline phosphatase activity matured earlier than did disaccharidase activity. Mucosal enzymes other than alkaline phosphatase were virtually absent from meconium and the large intestine. Continued ingestion of lactose could be detrimental in foals suffering from severe diarrhoea.
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PMID:The development and distribution of mucosal enzymes in the small intestine of the fetus and young foal. 106 Aug 71

The milk components lactose and casein enhance the apparent absorption of magnesium and possibly also of calcium, whereas phytate, which occurs in soya-bean products, has an inhibitory effect. This implies that soya-bean beverage v. cow's milk could lower bioavailability of Mg and Ca. This hypothesis was tested in two experiments with growing rats. Feeding soya-bean beverage v. cow's milk consistently lowered body-weight gain, enhanced bone turnover, as measured by increased plasma alkaline phosphatase (EC 3.1.3.1) activity and increased urinary hydroxyproline excretion, and decreased Mg and Ca concentrations in the femur. Because the mineral compositions of the soya-bean beverage and the cow's milk were different, the intake of Mg was higher in rats fed on soya-bean beverage, whereas that of Ca was higher in rats fed on cow's milk. Supplementation of the soya-bean beverage either with phosphorus and Ca or with P, Ca and methionine, to concentrations identical to those in milk, restored growth and bone mineralization. When using diets carefully balanced for Mg, Ca, P, sodium, potassium and methionine, soya-bean beverage v. cow's milk in the diets decreased apparent absorption and urinary excretion of Mg and Ca. Hydrolysis of lactose in milk decreased absorption and urinary excretion of Mg; it did not significantly affect Ca absorption but lowered urinary Ca excretion. The present study shows that soya-bean beverage v. milk depresses Mg and Ca bioavailability, as would be predicted on the basis of reported effects of their purified components.
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PMID:Bioavailability of magnesium and calcium from cow's milk and soya-bean beverage in rats. 139 Jun 10

A study of the cavitary and membrane digestion of lipids, carbohydrates, proteins and data of the histological structure of the bioptate of the duodenal mucosa in 34 patients with chronic pancreatitis revealed the morphological picture of chronic duodenitis. This resulted in a reduction of the sorption properties of the intestinal epithelium that was manifested in a reduction of the rate of membranous digestion, mainly of lipids and lactose. Lesser degrees of protein, starch and saccharose hydrolysis were observed. Biopsy specimens of the duodenal mucosa showed a reduced activity of enterokinase and alkaline phosphatase. Antacids (almagel, phosphalugel), mineral waters ("Borzhomi", "Poliana Kvasova"), regeneration stimulators (Metacyl, retalil), agents stimulating the motor function (cerukal, reglan and oth.) are recommended for the complex treatment of concomitant duodenitis.
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PMID:[The functional-morphological changes in the duodenum in chronic pancreatitis]. 147 21

A group of four rhi (rhizosphere-expressed) genes from the symbiotic plasmid of Rhizobium leguminosarum biovar viciae has been characterized. Although mutation of the rhi genes does not normally affect nodulation, in the absence of the closely linked nodulation genes nodFEL, mutations in the rhi genes can influence the nodulation of the vetch Vicia hirsuta. The DNA sequence of the rhi gene region reveals four large open reading frames, three of them constituting an operon (rhiABC) transcribed convergently toward the fourth gene, rhiR. rhiABC are under the positive control of RhiR, the expression of which is repressed by flavonoids that normally induce nod gene expression. This repression, which requires the nodD gene product (the transcriptional activator of nod gene expression), may be due to a cis effect caused by a high level of NodD-dependent expression from the adjacent nodO promoter, which is transcribed divergently from rhiR. RhiR shows significant similarities to a subfamily of transcriptional regulators that includes the LuxR and UvrC-28K proteins. RhiA shows limited homology to a short domain of the lactose permease, LacY, close to a region thought to be involved in substrate binding. No strong homologies were found for the other rhi gene products. It appears that RhiA and RhiB are cytoplasmic, whereas RhiC is a periplasmic protein, since it has a typical N-terminal transit sequence and a rhiC-phoA protein fusion expresses alkaline phosphatase activity. The biochemical role of the rhi genes has not been established, but it appears that they may play a role in the plant-microbe interaction, possibly by allowing the bacteria to metabolize a plant-made metabolite.
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PMID:Molecular characterization and regulation of the rhizosphere-expressed genes rhiABCR that can influence nodulation by Rhizobium leguminosarum biovar viciae. 159 18


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