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:3.1.3.1 (alkaline phosphatase)
47,916 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Purified chondrocytic alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) from bovine fetal epiphyseal cartilage hydrolyzes a variety of phosphate esters as well as ATP and inorganic pyrophosphate. Optimal activities for p-nitrophenyl phosphate, ATP and inorganic pyrophosphate are found at pH 10.5, 10.0 and 8.5, respectively. The latter two substrates exhibit substrate inhibition at high concentrations. p-Nitrophenyl phosphate demonstrates decreasing pH optima with decreasng substrate concentration. Heat inactivation studies indicate that both phosphorolytic and pyrophosphorolytic cleavage occur at the same site on the enzyme. Mg2+ (0.1-10.0 mM) and Mn2+ (0.01-0.1 mM) show a small stimulation of p-nitrophenyl phosphate-splitting activity at pH 10.5. Levamisole, Pi, CN-, Zn2+ and L-phenylalanine are all reversible inhibitors of the phosphomonoesterase activity. Pi is a competitive inhibitor with a Ki of 10.0 mM. Levamisole and Zn2+ are potent non-competitive inhibitors with inhibition constants of 0.05 and 0.04 mM, respectively. The chondrocytic alkaline phosphatase is inhibited irreversibly by Be2+, EDTA, EGTA, ethane-1-hydroxydiphosphonate, dichloromethane diphosphonate, L-cysteine, phenyl-methylsulfonyl fluoride, N-ethylmaleimide and iodoacetamide. NaCL, KCL and Na2SO4 at 0.5-1.0 M inhibit the enzyme. At pH 8.5, the cleavage of inorganic pyrophosphate (pyrophosphate phosphohydrolase, EC 3.6.1.1) by the chondrocytic enzyme is slightly enhanced by low levels of Mg2+ and depressed by concentrations higher than 1mM. Ca2+ show only inhibition. Similar effects of Mg2+ and Ca2+ on the associated ATPase (ATP phosphohydrolase, EC 3.1.6.3) activity were observed. Arrhenius studies using p-nitrophenyl phosphate and AMP as substrates have accounted for the ten-fold difference in V in terms of small differences in both the enthalpies and entropies of activation which are 700 cal/mol and 2.3 cal/degree per mol, respectively.
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PMID:Enzymatic characterization of the chondrocytic alkaline phosphatase isolated from bovine fetal epiphyseal cartilage. 4 Jun 3

Eosinophilic leukocytes may accompany a great variety of disorders and different types of acute leukemias. The most striking morphologic feature of eosinophils is their specific granules, but morphology alone often is insufficient to differentiate normal from abnormal eosinophils. Cytochemically, the eosinophils were considered "normal" when they did not contain alkaline phosphatase, chloroacetate esterase, toluidine blue metachromasia, Astra blue positivity, and specific PAS-positive granules, but did have peroxidase and cyanide-resistant peroxidase activities, Sudan black positivity and moderate naphthol-AS esterase or alpha-naphthyl esterase and acid phosphatase positivities. In seven cases of acute leukemias (two acute myeloblastic and five myelomonocytic), in contrast with their normal behaviour, the eosinophils show "abnormal" cytochemical positivities consisting of chloroesterase activity, PAS and Astra blue positivities of the specific granules, toluidine blue metachromasia, and cyanide-resistant peroxidase of a few specific granules. Cytochemical investigations may provide additional criteria for evaluating the abnormality of the eosinophilic cell in leukemias.
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PMID:Cytochemical "normal" and "abnormal" eosinophils in acute leukemias. 7 Jan 68

The properties of a highly purified inorganic pyrophosphatase (pyrophosphate phosphohydrolase; EC 3.6.1.1) from pig scapula cartilage were studied. The enzyme had a molecular weight of 66 000 and a pH optimum of 7-8. It was markedly activated by magnesium, but not, or only to a much smaller degree, by other metal ions. PP1 was the only substrate found and had a Km value of 11 muM. The enzyme was not inhibited by phosphate and other inhibitors of alkaline phosphatase such as CN- minus, amino acids and theophylline; it was slightly inhibited by tartrate, formaldehyde and ammonium molybdate and strongly inhibited by F- minus, Ca2+ and other metal ions. The properties of the enzyme in the presence of concentrations of PP1 present in plasma (3.5 muM) were similar to those found at higher (2 mM) concentrations of PP1. The diphosphonates ethane-1-hydroxy-1,1-diphosphonate and dichloromethylenediphosphonate inhibited the enzyme in the presence of low PP1 concentrations. The characteristics of this enzyme are therefore similar to pyrophosphatases from other sources, such as from yeast and erythrocytes, and do not support a specific role of this enzyme in the calcification process.
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PMID:Properties of inorganic pyrophosphatase of pig scapula cartilage. 23 96

The regenerating forelimb of the adult newt, Notophthalmus viridescens was investigated for 5'-nucleotidase (5' ribonucleotide phosphohydrolase, 3.1.3.5) acitivity. The newt's humeri were surgically removed, and after a twenty-one-day recovery period, the forelimbs amputated above the elbows. Regenerates were sampled at predetermined times for specific phases in the progress of regeneration, frozen, sectioned in a cryostat, and the sections fixed in 10% cold formol calcium. The Wachstein and Meisel [25] lead procedure at neutral pH was used predominately in these experiments, although tests were also conducted with Gomori's [14] calcium, Allen's [21] highly alkaline procedures. The substrates used to obtain specific enzyme reactions were adenine, cytosine, guanine, uracil and inosine 5'-monophosphate nucleotides. Sodium beta-glycerophosphate served as a non-specific phosphomonoesterase substrate, distilled water replaced substrate, and inhibitors such as zinc and cyanide ions were used as control measures to assist in increasing the precision in interpreting the results obtained. The most reactive 5'-nucleotidase (5'-Nase) loci were in the walls of the blood vascular system, mysial and neural sheaths, dermis, and periosteum: the principal cells involved were macrophages, endothelium of blood vessels, and fibrocytes of connective tissues. A moderate enzyme response was elicited from secretory cells of some of the subcutaneous glands, hypertrophied chondrocytes and osteogenic centers, chondrocytes in the articular regions and within red blood cells and leucocytes. Normal, injured and degenerating, or regenerating striated muscle and nerve fibers were judged unreactive for 5'-Nase. The epidermis and wound epithelium displayed negative responses for 5'-Nase. Cells forming the regeneration blastema were 5'-Nase reactive during the early formative phase, but with growth and development of the blastema into bulb and conic forms, these cells did not respond for this enzyme-activity. One suggestion offered is that the absence of 5'-Nase in cells of the blastema may be related to the lack of an adequate blood-vascular supply. Several functions of 5'-Nase in normal and regenerating tissues are discussed. A basic conclusion reached is that 5'-nucleotidase hydrolyses may be more involved in fundamental anabolic than in catabolic metabolism.
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PMID:Localization of 5'-ribonucleotide phosphohydrolase in regenerating (and normal) limb tissues of the adult newt Notophthalmus viridescens. 24 77

Some properties and the intracellular distriubtion of inorganic pyrophosphatase in rabbit dental pulp were determined. This enzyme was sensitive to Mg2+, and not inhibited by imidazol and CN- which are inhibitors of alkaline phosphatase. Inorganic pyrophosphatase was found predominantly in the supernatant fraction.
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PMID:Properties and distribution of inorganic pyrophosphatase in rabbit dental pulp. 27 89

Human liver alkaline phosphatase is a metalloenzyme requiring Zn2 and Mg2 for full activity. Zn2 cannot be replaced by manganese, cobalt or calcium, whereas Mg2 can be replaced by manganese or calcium. The binding constants of the enzyme for different divalent cations were determined by the use of complexing agents. The enzyme is inhibited by a number of reducing and complexing agents such as 2-mercaptoethanol, cyanide, nitrilotriacetic acid and EDTA. From studies using these inhibitors it is suggested that there are different mechanisms of inhibition. Reversible inhibition occurs if the free Zn2 concentration is not significantly lower than 10(-12)M. Inhibition is irreversible at lower Zn2 concentrations. Evidence is given, that the human liver alkaline phosphatase possesses different zinc binding sites, which are responsible for the catalytic function and for the integrity of the enzyme structure.
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PMID:Human alkaline phosphatases. II. Metalloenzyme properties of the enzyme from human liver. 92 71

Tissue factor content of WISH amnion cells in spinner culture increases 3- to 10-fold within 12 hours after subculture, then declines to a basal level within 30 to 50 hours. Maximal development of activity requires fresh serum and fresh medium. When added at the time of subculture, actinomycin D and cycloheximide completely inhibit development of coagulant activity; when added several hours after transfer, these inhibitors suppress the development but do not affect the disappearance of activity. Of the oxidative phosphorylation inhibitors tested, dinitrophenol had no effect whereas carbonyl cyanide m-chlorophenylhydrazone inhibited the activity increase but did not alter the decline. The kinetics of development and decay are similar over a pH range of 6.7 to 7.6 and with fetal calf serum concentration between 5 and 30 per cent. At pH 6.7 or in 30 per cent fetal calf serum, cell division did not occur. 3H-leucine and 35SO4= incorporation into the cell surface coat did not change appreciably during the burst of coagulant activity nor did the levels of naphthylamidase or alkaline phosphatase; 3H-thymidine incorporation reached a peak within 2 hours of the tissue factor maximum.
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PMID:Tissue factor in cultured cells: metabolic control. 103 35

Subcellular distribution study of cytoplasmic organelles was performed on human polymorphonuclear leukocytes after homogenization in 0.34 molar sucrose by differential centrifugation and sucrose density gradient centrifugation of the homogenate. The whole homogenate and each fraction was assayed for nitroblue tetrazolium (NBT)-reductase with and without 1 mM potassium cyanide, and the distribution of this enzyme was compared to the distribution of lysozyme, peroxidase, beta-glucuronidase, and acid and alkaline phosphatase. Enzyme recovery was 97 per cent and ranged between 74 and 124 per cent. Latent activity of all enzymes except NBT-reductase, acid, and alkaline phosphatase was demonstrated by observing a four- to sixfold increase in activity after the addition of Triton-X 100. Maximal relative specific activity using either DPNH or without cyanide for NBT-reductase was found in the 100,000 x g differential centrifugation fraction and was concentrated in the less dense top fraction of the sucrose density gradient. The distribution pattern was similar to acid and alkaline phosphatase. In contrast, the maximal concentration of beta-glucuronidase and peroxidase was found in the heavier 7,200 x g granule fraction and in the more dense bottom fractions of the sucrose density gradient. Maximal lysozyme activity was concentrated in the 30,000 x g granule fraction and in the fractions located between the heaviest and lightest fractions of the sucrose density gradient. The lack of latent activity and the similarity of subcellular distribution of NBT-reductase to acid and alkaline phosphatase, two enzymes associated with microsomes and plasmalemal membranes in human polymorphonuclear leukocytes (PMN), indicates that NBT-reductase is also a nonlysosomal enzyme located in microsomes or in plasmalemal membranes. These findings support the previously described histochemical observations that initial reduction of NBT to formazan occurs on the PMN plasmalemal surface membrane at the point of particle attachment. In addition, they suggest that alteration of the surface membrane of the PMN by particle attachment or other surface forces may activate NBT-reductase, leading to an accumulation of formazan in the region of the altered membrane as the phagocytic vacuole is formed.
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PMID:Subcellular distribution of nitroblue tetrazolium reductase (NBT-R) in human polymorphonuclear leukocytes (PMN). 118 38

Experiments were carried out to study the digestibility of a cassava (gari) diet and its effect on growth in young male dogs. Three groups of dogs were fed on diets with rice (control), cassava (gari), and rice + cyanide respectively as the carbohydrate source. Each diet contained 130 g crude protein (nitrogen x 6.25)/kg, was supplemented with vitamins and minerals, and was fed for 14 weeks. Variables measured were body-weight gain, bone growth, plasma alkaline phosphatase (EC 3.1.3.1) activity, total serum 3,5,3'-triiodothyronine (T3) and some plasma free amino acids. The apparent digestibilities of dry matter, protein and fat were not significantly different in the three groups, but the digestibility of gari fibre was significantly lower than the digestibility of rice fibre when fed to dogs (P less than 0.05). Proximate analysis of the faeces showed that the group of dogs fed on the gari diet had faeces which had a significantly higher moisture content than the faeces of the other groups (P less than 0.05), and also a significantly higher fibre content (P less than 0.05). There was no significant difference in body-weight gain and bone growth between the control and gari-fed groups of dogs, but these variables were significantly lower in the dogs fed on the rice + cyanide diet (P less than 0.05). At the end of the 14-week experimental period total serum T3 and plasma alkaline phosphatase activity were not significantly different between the control group of dogs and the gari-fed group, but were significantly lower in the rice + cyanide group. Plasma free methionine, leucine, isoleucine and valine concentrations were higher in the rice + cyanide group of dogs than in the control group and the gari group, indicating that these amino acids were accumulating and not being utilized for protein synthesis and growth to the same extent in the rice + cyanide group of dogs as in the other groups. It was concluded that the digestibilities of cassava starch and rice starch were the same in the dog but that rice fibre was more digestible in the dog than cassava fibre. It was also concluded that growth proceeded normally when a balanced gari diet or a balanced rice diet containing 130 g crude protein/kg was fed to dogs, but growth was retarded when a balanced rice + cyanide diet containing 130 g crude protein/kg was fed to dogs because total serum T3 concentration became greatly depressed.
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PMID:Digestibility of a nutritionally-balanced cassava (Manihot esculenta Crantz) diet and its effect on growth in young male dogs. 166 68

Alkaline phosphatase activity in rat hepatoma cells (R-Y121B) cultured in a monolayer at 0.5% serum was enhanced by serum, bovine serum albumin, casein and gamma-globulin, but ovalbumin, polyvinylpyrrolidone, dexamethasone, insulin and dibutyrylcyclic AMP showed little effect on alkaline phosphatase activity. In addition, cycloheximide, actinomycin D, chloroquine, dinitrophenol and potassium cyanide also increased the enzyme activity, although the incorporation of [14C]leucine into cellular proteins was almost completely inhibited in the presence of these cytotoxic substances. When R-Y121B cell homogenates were incubated at 37 degrees C, alkaline phosphatase activity increased in a pH-dependent manner: the maximal increase was observed at pH 7.1. The magnitudes of the increase differed among cell homogenates and a 4- to 10-fold increase was observed. Alkaline phosphatase in R-Y121B cells was apparently heat-stable, but that in the cells obtained from various treatments was heat labile and the latter activity decreased to less than 50% of the initial activity after 15 min of incubation at 56 degrees C. Alkaline phosphatase in the control and also in the treated cells was more sensitive to L-homoarginine than L-phenylalanine. The Lineweaver-Burk plot showed that the increases in the enzyme activity were accompanied by changes not only in V but also in Km for alkaline phosphatase reaction. Finally, it has been suggested that the increases in alkaline phosphatase activity under various conditions are due to the conversion of the molecule with a low enzyme activity to the molecule with a high enzyme activity in R-Y121B cells.
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PMID:Regulation of alkaline phosphatase activity in rat hepatoma cells. Effects of serum proteins, cycloheximide, actinomycin D, chloroquine, dinitrophenol and potassium cyanide. 241 85


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