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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 binding of metal to alkaline phosphatase from Escherichia coli and the binding of water and orthophosphate to the Me-2+-enzyme binary complex have been examined by water proton relaxation rate (PRR) measurements. Titration of the three paramagnetic metals, Mn2+, Cu2+, and Co2+, into apoalkaline phosphatase and the titrations of apoenzyme into metal have been carried out. Analysis of the spin-lattice relaxation rates for these titrations and of Scatchard binding curves derived from these results, as well as EPR data, show four tight manganese sites, between two and three tight copper sites, or four cobalt sites per enzyme dimer of molecular weight 80,000. The multiple sites for each metal are indistinguishable by these magnetic resonance techniques. Both the spin-lattice- and spin-spin-relaxation rates exhibit a negative temperature coefficient, showing that these processes are not exchange-limited. From a frequency dependence study of T-1 and from the T-1:T-2 ratio measured at 220 MHz, correlation times from the water-enzyme complexes have been estimated. For H20-Mn-2+-alkaline phosphatase, gamma c equals 1.55 times 10-9 s; for H20-Cu-2+ -alkaline phosphatase, gamma c equals 1.82 times 10-s; and for the cobalt complex, gamma c equals 1.0 times 10-12 s at 4 degrees. Assuming 1 water molecule bound per metal site, these correlation times correspond to the following water-metal distances: gamma (A) is 4.0 A for Mn-2+-H20, 3.4 A for Cu-2+-H20, and 2.8 A for Co-2+-H20. Thus, water is shown to bind directly to the metal atoms of alkaline phosphatase. The correlation between the length of the water-metal bond and the relative activity of the various metalloenzymes support the importance of this binding in the monophosphoesterase reaction catalyzed by alkaline phosphatase. Addition of excess orthophosphate to any of the water-metalloenzyme complexes does not displace an exchangeable water molecule from the metal site. The Mn-PO-4 distance which we have reported earlier (Zukin, R.S., Hollis, D.P., and Gray, G.A. (1973) Biochem. Biophys. Res. Commun. 53, 238) to be 7.3 A is consistent with this finding and suggests a model in which Pi binds to Mn-2+-alkaline phosphatase through a water bridge.
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PMID:Role of metal ions in Escherichia coli alkaline phosphatase. A study of the metal-water interaction by nuclear relaxation rate measurements on water protons. 16 41

Literature on the biochemical effects of oral contraceptives (OCs) is reviewed. The effects of OCs on concentrations of mineral elements ( calcium, phosphorus, magnesium, iron, copper, and zinc), vitamins (ascor bic acid, folic acid, and Vitamins-B6, B12, and E), hormones, (gonadotro pins, progesterone, estrogens, androgens, corticosteroids, aldosterone, renin-angiotensin, insulin, growth hormone, thyroid hormones, catecholamines, and prolactin), amino acids and proteins (free amino acids, tryptophan, metalloproteins, hormone-binding proteins, miscellaneous serum proteins, and blood coagulation factors), carbohydra tes (glucose tolerance tests, glucose metablism and other carbohydrates) , lipids (total serum lipids, triglycerides, phospholipids, fatty acids, and cholesterol), and enzymes (aminotransfereases, alkaline phosphatase, and glutamyltransferase) are reviewed. Changes induced by combined, sequential, and low-dose OCs in 116 biochemical parameters are summarized in a table.
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PMID:Biochemical effects of oral contraceptives. 18 Jul 84

The rate of p-nitrophenyl phosphate and flavin mononucleotide (FMN) hydrolysis by the partially purified preparation of alkaline phosphatase I of Pichia guilliermondii flavinogenic yeast was studied as affected by different substrates and inorganic ions. Their Km was established to be 2.0 X 10(-4) m and 2.5 X 10(-4) M, respectively. Dephosphorylation of p-nitrophenylphosphate and FMN was inhibited competitively by beta-glycerophosphate (Ki = 3.1 X 10(-3) M, respectively). The presence of inorganic phosphate ions in the reaction mixture decreases or removes inhibition of these compounds hydrolysis by other substrates of alkaline phosphatase I. The activity of alkaline phosphatase I increases in the presence of Mg2+ and was strongly inhibited in the presence of Be2+, Cu2+, Zn2+, Cd2+ and inorganic phosphate, the mixture of Be2+ and F- being the most effective. This mixture inhibited the phosphatase activity of the partially purified preparation of alkaline phosphatase I of the cell-free extract as well as of intact cells in both the alkaline and acid zones of pH (8.6 and 5.5, respectively). Incubation of the washed iron-deficient P. guilliermondii cells in the presence of Be2+ and F- did not result in accumulation of FMN in the yeast culture. A possible role of nonspecific phosphomonoesterases in hydrolysis of FMN in vivo is discussed.
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PMID:[Inhibition of alkaline phosphatase I of Pichia guilliermondii yeast in vitro and in vivo]. 20 3

Extracts of adult Paramphistomum explanatum have been shown to contain high concentration of acid phosphomonoesterase with maximum activity at pH 4.5. The enzyme has been characterized by an exhibition of an unexpected increase in the inhibitory action of a mercury at 1 mM concentration by EDTA. With a lower concentration of mercury (0.1 mM and below) EDTA gave partial protection against inhibition. Different concentrations of magnesium and cobalt activated the enzyme while fluoride, copper, arsenate, tartrate and p-mercuribenzoate brought about inhibition. EDTA, glycine, glutathione and sodium azide had no effect. There was an indication of the presence of alkaline phosphomonoesterase at pH 10.0. The Km for p-nitrophenyl phosphate hydrolysis was 0.45 mM at pH 4.5.
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PMID:Phosphatase systems in Paramphistomum explanatum Fischoeder, 1901. 23 47

15 cases of histiocytosis X and 274 cases of histologically confirmed sarcoidosis were diagnosed during the investigation period from 1969 to 1975. Data of 12 adults with primary pulmonary histiocytosis X were evaluated in extenso. The necessary histological verification of diagnosis was only possible by open lung biopsy. Already in early stage small excavations were found by tomography in half of the cases. Eelvation of serum copper and of the index of leukocyte alkaline phosphatase was striking. In a single case antinuclear antibodies were proven. An intra patient comparison verifies corticosteroids suppressing the disease. On the occasion of a second lung biopsy in one case could be seen that after treatment no more histiocytosis-specific substrate was existing. Exacerbation and relapse during and after continuous long-term therapy were not observed. The features of histiocytosis X and sarcoidosis are set side by side in order to show differences and relations.
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PMID:[Special diagnostic and therapeutic aspects of pulmonary histiocytosis X in twelve cases from 1969 to 1975 (author's transl)]. 30 28

Midgut glands of abalone Haliotis discus contained two acid phosphatases [orthophosphoric-monoester phosphohydrolase (acid optimum), EC 3.1.3.2] separable by phosphocellulose column chromatography. They were designated as acid phosphatases I and II in order of elution and were purified 99- and 290-fold, respectively. Purified acid phosphatase II was nearly homogeneous as judged by polyacrylamide gel electrophoresis. The substrate specificity of acid phosphatase I was narrow, whereas that of acid phosphatase II was broad. Good substrates for acid phosphatase I included p-nitrophenyl phosphate, phosphoenolpyruvate, inorganic pyrophosphate, and nucleoside di- and triphosphates. The acid phosphatases did not require any metal ion for maximum activity and were inhibited by Zn2+, Cu2+ and Hg2+. Fluoride and arsenate were potent inhibitors of both enzymes. The pH optima of acid phosphatases I and II were 5.9 and 5.5, respectively. The molecular weights of acid phosphatases I and II were estimated to be 28,000 and 100,000, respectively, by gel filtration on Sephadex G-100. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis suggested that acid phosphatase II consists of two identical subunits.
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PMID:Purification and properties of two acid phosphatases from midgut glands of abalone Haliotis discus. 40 32

The safety and effectiveness of sodium cellulose phosphate (SCP) in the treatment of calcium urolithiasis of absorptive hypercalciuria was explored. Eighteen patients with absorptive hypercalciuria with intestinal hyperabsorption of calcium, normal or suppressed parathyroid function, and active stone disease received 10 to 15 Gm SCP daily (2.5 to 5 Gm with meals) and 2 to 3 Gm magnesium gluconate daily (1 to 1.5 Gm twice daily orally separately from SCP) for eight to 54 months, while maintained on a moderate calcium and oxalate restriction. During treatment, serum calcium, immunoreactive parathyroid hormone, and urinary cyclic AMP remained within the normal range. Serum alkaline phosphatase and bone density (measured by photon absorptiometry) did not change significantly or remained within normal limits. Serum concentrations of magnesium, copper, zinc, and iron and blood hematocrit were not significantly altered by therapy. However, urinary calcium returned toward normal, and incidence of renal stone formation markedly decreased. The results suggest that SCP is a safe and an effective drug for absorptive hypercalciuria.
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PMID:Clinical pharmacology of sodium cellulose phosphate. 48 64

The above problem was studied by furnishing four groups of six gilts each with ear catheters for the following intravenous catheter treatment: 2,500 IU heparin per die over ten days, supported by two daily oral applications of 1 g Falithrom, or 2,500 IU heparin plus two daily applications of 1 g Falithrom, all intravenously. The last group remained untreated for control. One day of the dioestrus was chosen for catheter bleeding of all animals at 6 a.m., 8 a.m., noon, and 4 p.m. and subsequent determination from the plasma of free fatty acids, copper, inorganic phosphorus, total protein, albumin, globulin, chloride, urea, cholesterol, alkaline phosphatase, blood sugar, and beta-lipoproteides. Significant differences regarding these parameters between the various groups were not even established, if alpha = 0.25. The anticoagulants used in the study may be used without any reservation for catheter rinsing and clearing and will not cause any significant change in the levels of the blood parameters.
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PMID:[Effect of anticoagulants on the change of blood parameters in diestric gilts]. 56 72

The precision and accuracy of 21 methods in clinical chemistry (sodium, potassium, calcium, chloride, phosphorus, iron, copper, bilirubin, uric acid, urea, creatinine, total serum protein, triglycerides, glutamate-oxalacetate-transaminase, glutamate-pyruvate-transaminase, alpha-hydroxybutyrate-dehydrogenase, alkaline phosphatase, lactate dehydrogenase, gamma-glutamyl-transpeptidase, acid phosphatase, amylase) were studied after diluting samples 1 : 2 and 1 : 4. Dilution of 1 : 2 did not show any significant effect on the precision and accuracy of the studied methods. In case of chloride, phosphorus, iron, bilirubin, uric acid, urea, creatinine, total serum protein, triglycerides, glutamate-oxalacetate-transaminase and alkaline phosphatase reliable results were obtained also after 1 : 4 dilution.
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PMID:[Precision and accuracy of 21 methods in clinical chemistry using diluted samples (author's transl)]. 56 36

Six pyridine-2-carboxaldehyde, one pyridine N-oxide 2-carboxaldehyde, and five diketone thiophosphoric hydrazones, three thiophosphoric hydrazides, and two cupric chelates were synthesized. The chelates and nine of the hydrazones were tested against Ehrlich ascites carcinoma. Seven of these latter agents were administered concurrently with either cupric and/or ferrous salts to mice bearing this tumor. The greatest activity was found with the chelate, cimethyl pyridine-2-carboxyaldehyde phosphorothioic hydrazone-copper (1:1). The hydrazone portion of this chelate also formed a ligand-copper (2:1) complex. Although all of the hydrazones but one were inactive when evaluated alone, the concurrent injection of cupric ion increased survival times by an avoli alkaline phosphatase was found to be inhibited by two thiosemicarbazones in a manner similar to that previously reported by these agents against alkaline phosphatase derived from Sarcoma 180-6-thiopurine resistant ascites cells. None of the 14 hydrazides or hydrazones tested against E. coli enzyme displayed significant inhibition.
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PMID:Phosphorus-nitrogen compounds. 20. Thiophosphorus hydrazones. 78 82


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