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 ability of D-valine medium to inhibit fibroblasts in cultures derived from kidneys of various mammals has enabled the selective proliferation of epithlial cells in the absence of fibroblast overgrowth. Studies of these selected epithelial cells have demonstrated the presence of D-amino acid oxidase, carbonic anhydrase, high levels of alkaline phosphatase and the renal specific pattern of lactate dehydrogenase. The presence of these renal enzymes suggests that the selected epithelial cells are of renal tubular origin and indicates that these differentiated functions are retained in cultured cells.
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PMID:Renal enzymes in kidney cells selected by D-valine medium. 1 81

Blood pH, bicarbonate, PCO2, serum calcium, alkaline phosphatase and red cell carbonic anhydrase were measured in 37 selected patients receiving anticonvulsants. Patients with metabolic acidosis showed a high incidence of hypocalcemia with increased alkaline phosphatase and a significant reduction of carbonic anhydrase-B activity. High iPTH levels were found in 13 patients, but this was not correlated with acid-base balance status. Anticonvulsant drugs seemed to inactive carbonic anhydrase-B activity. Metabolic acidosis might be one of the factors causing a disturbance of calcium metabolism in these patients.
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PMID:Metabolic acidosis in patients receiving anticonvulsants. 4 17

Whole blood samples from 40 male and 40 female individuals were analyzed for zinc, copper, selenium and iron, and in part also for cadmium and lead. Correlations were established between the element contents and the activities of blood enzymes (carbo-anhydrase, leucine aminopeptidase, lactate dehydrogenase, alkaline phosphatase, glutathione peroxidase). The zinc-copper ratio exerted no effect on the zinc-dependent enzymes. There was a correlation between the glutathione peroxidase activity and the selenium content in whole blood (r greater than 0.73). A cluster analysis was performed. In women, the authors stated a significant effect of oral contraceptives especially on the zinc and copper balance. It was evidenced that detectable (more marked) changes in the mineral equilibrium are not produced in all cases by the contraceptives. Nevertheless, changes in the mineral equilibrium are likely to occur in 25% of all women. In the present study further changes (for example in enzymes) were observed in 50% of all women. The results obtained from the male individuals were indicative of certain relationships between the zinc-copper ratio and the content of total lipids or lipid fractions in human blood.
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PMID:[Effect of the trace element supply on element dependent enzymes in man]. 11 Nov 26

The thymidine analog, 5-bromodeoxyuridine (BrdU), inhibits the differentiation of the acinar cells of the embryonic rat pancreas, while having little effect on the growth of the tissue. The BrdU-treated pancreas contains elevated alkaline phosphatase and carbonic anhydrase activities, and, unlike the normal pancreas, contains numerous extracellular fluid-filled vacuoles, surrounded by ductlike cells. Both alkaline phosphatase and carbonic anhydrase activities are located preferentially in the ductlike cells lining the vacuoles. The biochemical, morphological, and functional features of these epithelial cells are therefore characteristic of the normal pancreatic duct cell. Thus, in the exocrine pancreas, BrdU seems to alter the normal program of differentiation by favoring the functional duct cells while inhibiting the differentiation of acinar cells.
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PMID:5-bromodeoxyuridine may alter the differentiative program of the embryonic pancreas. 13 50

Mg-dependent ATP-ase, alkaline phosphatase and carbonic anhydrase activities were tested at the level of capillary endothelia of alveolar walls in normal rabbits. A constant and relatively intense activity within these endothelia appeared to be that of the Mg-dependent ATP-ase. The carbonic anhydrase activity marked some endothelia, and the alkaline phosphatase was unequally demonstrable at this level. These different histoenzymic aspects might reflect the unequal activity during time and space of these enzymes at the level of capillary endothelia of alveolar walls.
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PMID:Histoenzymology of the lung. Some enzymic activities of capillary endothelia of the rabbit alveolar walls. 14 9

In this study, enzyme activities of the pancreatic appendages of the ductus hepatoPancreas (the so-called "pancreas") in Sepia officinalis L. have been demonstrated by light and electron micicroscopical methods: Malate dehydrogenase, monoamine oxidase, acid phosphatase, beta-glucuronidase, adenosine triphosphatase and carbonic anhydrase were shown by the former, and monoamine oxidase, catalase, glutamic oxalacetic transaminase, choline esterase (non-specific), alkaline phosphatase, acid phosphatase and carbonic anhydrase by the latter technique. The correlation between enzyme activity and distribution, and the presumed function of the two pancreatic epithelia is discussed.
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PMID:The localization of enzyme activities in the pancreatic appendages of Sepia officinalis L. (Cephalopoda). 15 95

The plasma membrane enzymes, alkaline phosphatase, bicarbonate-dependent adenosine triphosphatase, 5'-nucleotidase, and carbonate dehydratase, were measured in ductal and acinar preparations of bovine pancreas. Epithelial cells were scraped from the main duct and a piece of acinar tissue was dissected from the whole pancreas for homogenization. All enzymes studied demonstrated higher levels in the duct per milligram protein than in the acinus: bicarbonate-dependent adenosine triphosphatase was 2.8 times higher; 5'-nucleotidase, 4.1 times higher; carbonate dehydratase, 16.9 times higher, while alkaline phosphatase showed only a slight increase in the duct compared to acini.
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PMID:Enzymic profiles of bovine pancreatic ductal and acinar tissues. 15 38

The magnetic circular dichroic (MCD) spectra of cobalt(II) sugstituted metalloenzymes have been studied and compared to a series of four-, five-, and six-coordinate cobalt(II) model complexes previously examined (T. A. Kaden et al. (1974), Inorg. Chem. 13, 2582). The MCD spectra of cobalt substituted carboxypeptidase A, procarboxypeptidase ta, and thermolysin are consistent with earlier deductions of tetrahedral coordination from absorption spectra and also with X-ray structure analysis. Inhibitors fail to alter their MCD spectra significantly. The MCD spectra of cobalt alkaline phosphatase and carbonic anhydrase are more complex and their pH dependence and alteration by inhibitors are discussed in terms of known cobalt(II) models.
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PMID:Magnetic circular dichroic spectra of cobalt(II) substituted metalloenzymes. 23 52

For the purpose of detecting the synthesis of zinc metalloenzymes after zinc supplementation in an experiment using rats the animals were first depleted for 15 days and subsequently injected a labelled zinc salt solution (65Zn-ZnCl2) in a dosis of 0.4 mg (in terms of Zn) and with an activity of 3.0 muCi/100microliter. After a 5-day depletion period, the activity of the metallo-enzymes alkaline phosphatase in plasma and in the femur and carboxy-peptidase A and B in the pancreatic gland was found to rise at the same rate as the 65Zn-measuring rate in plasma, femur and pancreatic gland. By calculating correlations this interdependence was demonstrated. Thus the highly significant correlation coefficients prove for these metalloenzymes that a synthesis with the injected zinc salt has taken place whilst for carbo-anhydrase in blood this evidence was not furnished. As the zinc dosis is not exclusively used for the enzyme synthesis, but additional 65Zn is incorporated into the individual organs, it does not appear to be possible to draw conclusions from the 65 Zn-measuring rate in the individual organs on the intermediary availability.
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PMID:[Demonstration of zinc-metalloenzyme syntheses after zinc supplements for deficient animals by means of measurement of the incorporation of 65Zn in various organs]. 41 27

Several sulfonamides used as antibacterial or diuretic drugs are potent alkaline phosphatase inhibitors. The mechanism of inhibition may involve binding of the zinc in the active site of the enzyme by the unbonded electron pair on the sulfonamide group nitrogen atom as well as binding of the drug to a second site. Addition of progressively larger groups to this nitrogen leads to an increasing loss of inhibitory capability. Isoenzymes from human liver, bone, kidney, granulation tissue and intestine are inhibited to a similar extent while the placenta isoenzyme is more resistant. It is suggested that some pharmacologic actions of sulfonamides may be due to inhibition of alkaline phosphatase, rather than carbonic anhydrase.
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PMID:Sulfonamide inhibition of human alkaline phosphatase. 46 8


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