Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.8 (phytase)
 1,997 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Alkaline phosphatase, highly purified from bovine intestinal mucosa, has significant hydrolytic activity against phytate and CaATP. Phytase and CaATPase activities require quite different assay conditions than those which are optimal for conventional alkaline phosphatase substrates such as 4-nitrophenyl phosphate. We have used affinity chromatography and antibody recognition to demonstrate that the phytase and CaATPase activities are not due to contaminating enzymes, but are intrinsic activities of intestinal alkaline phosphatase. All of the phytase and CaATPase activities present in crude extracts of bovine intestinal mucosa can be accounted for by alkaline phosphatase. Apparently neither phytase nor CaATPase exist in this tissue as independent enzymes. Specific substrates which require assay conditions quite different from the conventional 4-nitrophenyl phosphate substrate may account for the physiological function of "alkaline phosphatase."
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PMID:The relationship of alkaline phosphatase, CaATPase, and phytase. 299 87

1. The effects of phosphorus deprivation on phytate digestibility, phosphorus utilization and intestinal phytase (EC 3.1.3.8) and alkaline phosphatase (EC 3.1.3.1) in rats were investigated. 2. P deprivation was achieved by giving rats a diet containing 3 g P/kg and resulted in hypophosphataemia, hypercalcaemia, hypercalciuria, and lower levels of P absorbed and retained, and calcium retained. 3. Rats adapted to P deprivation by increasing the digestion of total dietary-P and phytate-P. 4. Levels of intestinal alkaline phosphatase and alkaline phytase were not different between the two treatment groups. 5. P deprivation in the rats given the marginal-P diet may be a result of a lower absorption of total dietary-P or increased absorption of inositol phosphates formed during the enzymatic hydrolysis of phytate which are not readily utilized by the rat. 6. These results suggest that intestinal phytase and alkaline phosphatase do not play a role in the adaptive increase in phytate digestibility by rats given marginal-P diets. The adaptation may result from enhanced phytase or alkaline phosphatase synthesis by the gastrointestinal microflora stimulated by a lower level of P in the digesta.
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PMID:Adaptive increase in phytate digestibility by phosphorus-deprived rats and the relationship of intestinal phytase (EC 3.1.3.8) and alkaline phosphatase (EC 3.1.3.1) to phytate utilization. 629 37

Phosphatase activities associated with the intestinal brush border membrane (BBM) of the rat were examined histochemically in relation to the characteristic environment of the intestine, where luminal pH fluctuates drastically between alkaline and acid pH ranges. Special attention was given to intestinal alkaline phosphatase (IALP) and phytase on the BBM. Whole body fresh-frozen sections of young rats and their rapidly frozen and freeze-substituted small intestines, embedded in Technovit 7100, were processed for the histochemical demonstration of phosphatase activity at three different pH values (9.2, 7.3, and 5.2), representing the deviation of luminal pH in vivo. Either an azo-dye method or lead-salt method was employed using naphthol AS-MX phosphate and ATP as substrate, respectively. With the azo-dye method, intense phosphatase reactions were demonstrated along the BBM at all three pH ranges. Phosphatase reactions of the BBM at pH 9.2 and 7.3 were abolished by L(+)-phenylalanine, heat pre-treatment, and EDTA chelation although some reaction remained at pH 7.3 after the treatment with EDTA or L(+)-phenylalanine. Phosphatase reactions of the BBM at pH 5.2 were resistant to L(+)-phenylalanine, L(+)-tartrate, PCMB and EDTA chelation, implying that the characteristics of the enzyme responsible for phosphohydrolysis at acid pH values differed from those at higher pH values. The lead-salt method in which ATP was used as substrate revealed intense reactions--which were dependent on Mg++ and stimulated by Ca++ and resistant to L(+)phenylalanine--to be localized along the BBM at alkaline and neutral pH values, but not at acid pH values. In vitro experiments showed progressive hydrolysis of naphthol AS-MX phosphate by purified phytase at pH 5.2, in a dose-dependent manner, and suggested the possible involvement of phytase in the phosphatase reactions of the BBM at acid pH. These data indicate that the phosphatase reactions at alkaline and neutral pH values, associated with the BBM of the rat intestine, represent IALP and Mg++/ Ca++-ATPase, while those at acid pH appear to correspond to phytase activity, something which has not been demonstrated by histochemical methods despite the availability of extensive data based on biochemical analyses.
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PMID:Phosphatase activities of rat intestinal enterocytes and their relation to diverse luminal pH, with special references to the possible localization of phytase along the brush border membrane. 1183 8

An experiment was conducted to evaluate phytase supplementation on growth, phytate degradation, and the gene expression of myo-inositol transporters in 21-day old broilers. Ross 308, male broilers (n = 240) were assigned to one of four diets, with 10 pens/diet and six birds/pen from day one to 21. The diets consisted of a negative control (NC) formulated to meet or exceed Ross 308 nutrient requirements, with the exception of calcium (Ca) and available P (avP), which were reduced by 0.16 and 0.15%, respectively. The NC diet was supplemented with 0, 500, 1,500, or 4,500 units/kg of phytase (FTU) to create four experimental diets. On day 21, all birds per pen were euthanized to obtain digesta and tissue samples for phytate degradation and gene expression. Data were analyzed as an analysis of variance using the fit model platform in JMP v 13.0. The model included phytase and significant means were separated using orthogonal linear and quadratic contrasts. Phytase supplementation increased gain (linear, P < 0.05). Phytate (iP6; quadratic, P < 0.05), phytate ester (iP5, iP4, iP3; quadratic, P < 0.05), and inositol (linear, P < 0.05) concentration in the gizzard was influenced by phytase supplementation. Phytate concentration decreased (linear, P < 0.05), iP5 or iP4 concentration increased and then decreased (quadratic, P < 0.05), and inositol concentration increased (quadratic, P < 0.05) in the ileal digesta as phytase supplementation increased in the diet. There was a tendency for the gene expression of the H+-dependent myo-inositol transporter, HMIT, to increase (linear, P < 0.05) in the ileum as phytase dose increased. Gene expression of the sodium-dependent myo-inositol transporter, SMIT2, increased in the jejunum (quadratic, P < 0.05) as phytase dose increased. Intestinal alkaline phosphatase expression increased (linear, P < 0.05) in the ileum as phytase supplementation increased in the diet. The influence of phytase on phytate, phytate esters, and inositol may influence intestinal alkaline phosphatase activity and the gene expression of myo-inositol transporters in the small intestine.
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PMID:Effect of phytase on growth performance, phytate degradation and gene expression of myo-inositol transporters in the small intestine, liver and kidney of 21 day old broilers. 2944 20