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)

At least three loci determine human alkaline phosphatases [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1]: one coding for the placental form of the enzyme, at least one coding for the intestinal forms, and at least one for the liver, bone, and kidney forms. The alkaline phosphatase in cell line D98/AH-2 has been characterized by inhibition, thermostability, and electrophoretic studies. It is intestinal in type and resembles the fetal intestinal form somewhat more closely than the adult intestinal form. Intestinal alkaline phosphatase was found in the related cell lines Detroit 98, D98/S, and D98/AH-R. No placental alkaline phosphatase could be detected in any of these cell lines. This series of cell lines are believed, on the basis of earlier investigations, to be HeLa in origin but other HeLa cell lines show placental alkaline phosphatase. Loss of expression of the placental alkaline phosphatase locus probably occurred prior to the separation of Detroit-98 from the lineage leading to other HeLa cell lines and this has persisted in the Detroit-98 derivatives D98/AH-2, D98/S, and D98/AH-R. Another possibility is that placental alkaline phosphatase expression only appeared in the HeLa lineage subsequent to the separation of Detroit-98.
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PMID:Human cell lines expressing intestinal alkaline phosphatase. 29 Oct 61

Alkaline phosphatases, which had a unique electrophoretic mobility on polyacrylamide gel electrophoresis, were found in hepatic tissue of a patient with liver cirrhosis. Enzymic and immunological properties of the enzymes examined on electropherogram were similar to those of a fetal intestinal-type alkaline phosphatase in hepatoma with respect to sensitivity to amino acids, heat stability, sensitivity to sodium dodecyl sulfate, and reactivity to anti-intestinal alkaline phosphatase antiserum. The enzymes seem to be a variant of a fetal intestinal alkaline phosphatase. The significance of occurrence of the enzymes in cirrhotic liver is discussed.
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PMID:Electrophoretic variant of fetal intestinal alkaline phosphatase in a patient with cirrhotic liver. 44 73

The effect of anions on the thermodynamic activation functions for a model enzyme, calf intestinal alkaline phosphatase (EC 3.1.3.1), have been studied in order to examine the role of protein hydration changes in establishing the energetics of enzyme catalysis. The influences of these anions on the activation volume (delta V) and activation free energy (delta G) reflected clear Hofmeister (lyotropic) series effects, in the order F- greater than Cl- greater than Br- greater than I- (order of increasing salting-out potential). A pronounced covariation was observed between the influences of these anions on Vmax, which is proportional to delta G, and on the negative activation volume of the reaction. Fluoride was able to counteract the influences of Br- and I- on both Vmax and delta V when combinations of these anions were employed. The effects of Br- and I- on Vmax and delta V were more pronounced at lower temperatures. The control delta V was increasingly negative at reduced temperatures. The effects of the neutral salts and propanol on delta V and delta G, as well as the effects of salting-in anions on the activation enthalpy and the negative activation entropy of the reaction, are consistent with a model which proposes that peptide groups or polar side chains on the native enzyme exergonically increase their exposure to solvent during the catalytic activation event. These conclusions are in accord with the known free energy, enthalpy, entropy, and volume changes which occur when model peptide groups are transferred between water and concentrated salt solutions. Consistent with the kinetic results, the fluorescence emission wavelength maximum of alkaline phosphatase increased in the presence of anions in the order F- greater than Cl- greater than Br- greater than I-. The salting-out ion (F-) and the salting-in ions (Br- and I-) shifted lambda max in different directions, and these lambda max shifts could be counterbalanced by using equimolar combinations of salting-in and salting-out anions. Control experiments with a model compound, N-acetyltryptophanamide, showed that the spectra shifts caused by the salts did not result solely from differential quenching by the anions of the solvent-exposed tryptophan(s) on the enzyme. Hofmeister additivity phenomena indicated that the solvent is at the basis of these salt-induced enzyme structural changes. It is concluded that changes in protein solvation during enzymic reactions contribute significantly to the thermodynamic activation parameters in both the native and the salt-perturbed enzyme.
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PMID:Effects of anions on the activation thermodynamics and fluorescence emission spectrum of alkaline phosphatase: evidence for enzyme hydration changes during catalysis. 51 38

The proportions of the total activities of different isoenzymes of human alkaline phosphatase precipitated from serum by ethanol (20% v/v) were: liver phosphatase, 37%; placental phosphatase, 23%; bone phosphatase, 8.0%, and small-intestinal phosphatase, 3.7%. Treatment of the isoenzymes with neuraminidase reduced the percentages of non-intestinal phosphatases precipitated by ethanol to below 10%. Precipitation of intestinal alkaline phosphatase was unaffected by this treatment. The degree of solubility in ethanol therefore appears to be largely determined by the content of terminal sialic acid residues in the alkaline phosphatase molecules. In contrast the stabilities of the isoenzymes to heating at 56 degrees C were not significantly altered by neuraminidase digestion.
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PMID:Further observations on the differential precipitation of alkaline phosphatase isoenzymes by ethanol. 62 Apr 61

A procedure has been described whereby the high molecular weight alkaline phosphatase (slow-moving) isoenzyme may be studied by means of polyacrylamide gel electrophoresis. By treatment of sera containing this isoenzyme with some detergents of the nonionic Triton octylphenoxyethanol series, the high molecular weight alkaline phosphatase isoenzyme is altered so that its electrophoretic mobility more closely resembles that of the usual alklaine phosphatase isoenzymes. The high molecular weight isoenzyme is thought to be associated with phosphatidyl choline and/or liproproteins. The detergent action is to dissociated the alkaline phosphatase from its lipid carrier. It is thought that these lipid-alkaline phosphatase complexes are associated with liver cell fragments. The detergent altered slow-moving alkaline phosphatase may migrate as a single band, from two to four new bands, or as several new bands. Liver, bone and intestinal alkaline phosphatase isoenzymes are unaffected by detergent action.
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PMID:Detergent altered alkaline phosphatase patterns of liver disease. 62 28

Ethinyl estradiol treatment to female rats resulted in increased levels of serum alkaline phosphatase, but was not associated with any other manifestation of toxicity such as increased serum transaminases or toxic lesions. Elevated serum alkaline phosphatase seen in rats treated with chloroform was associated with frank hepatotoxicity. Induction of hepatic drug metabolising enzymes in rats by phenobarbitone treatment did not result in raised serum alkaline phosphatase levels. Estradiol benzoate treatment to rats also did not increase serum alkaline phosphatase levels. Ethinyl estradiol also resulted in increased alkaline phosphatase content in the liver, intestine and bone. The raised intestinal alkaline phosphatase content of rats treated with phenobarbitone or estradiol benzoate was not associated with an increase in the serum levels. There was histochemical evidence of induction of canalicular alkaline phosphatase in the liver in Ethinyl Estradiol treatment. The study of the electrophoretic separation of serum alkaline phosphatase of ethinyl estradiol treated rats revealed the presence of a new fast moving fraction, similar to those seen in bile duct ligated rats. It is concluded that the serum alkaline phosphatase increase during ethinyl estradiol treatment at least in part is from the liver, due to new synthesis.
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PMID:Serum alkaline phosphatase elevation in female rats treated with ethinyl estradiol. 67 18

The effect of pyridoxine deficiency was studied on the intestinal alkaline phosphatase of rat. Different segments of the intestine differed in their response to pyridoxine deficiency. In the duodenum alkaline phosphatase activity was decreased, whereas it was markedly increased in the ileum and the jejunal enzyme was least affected. The electrophoretic pattern of isoenzymes of alkaline phosphatase was altered in the ileum of B6 deficient rats.
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PMID:Effect of pyridoxine deficiency on rat intestinal alkaline phsophatase. 67 28

Alkaline phosphatase from human and calf small intestines has been prepared and purified until homogeneous, as judged by polyacrylamide gel electrophoresis, by means of the following techniques: n-butanol extraction, ammonium sulfate precipitation, acetone fractionation, ion exchange chromatography and isoelectric focusing in a sucrose density gradient. Three and two alkaline phosphatase froms from human and calf small intestines, respectively could be isolated by preparative isolectric focusing. The relative amounts of these components are not constant, but they have the same catalytic properties, suggesting that they may embody a common protein core with an identical active centre(s). Precipitating antisera for alkaline phosphatase from human and calf intestine have been prepard in rabbits by intramuscular, dermal, subcutaneous and intravenous administration of the pure major component of each enzyme species. Both antisera precipitate completely their homologous as well as their heterologous antigens (intestinal enzyme) and showed partial identity with placental alkaline phosphatase. There was no reaction with alkaline phosphatase from bone, liver heart, spleen, lung, stomach, pancreas, brain, bile-gall bladder and erythrocytes. Alkaline phosphatase preparation from human kidney contains a minor component of the intestinal type, beside many multiple forms which, on treatment with neuramindase, became identical in their electrophoretic and biochemical properties. At least eight multiple forms of the placental enzyme could be shown by isoelectric focusing in polyacrylamide gel. On treatment with neuraminidase these forms became less charged and only four forms remained. All forms were immunologically identical using either anti placental-enzyme or anti intestinal-AP serum. Monospecific antisera against human or calf intestinal alkaline phosphatase were obtained by absorption with purified placental enzyme. This monospecific anti intestinal-AP serum could be used for an immunological quantitative determination of the intestinal isoenzyme in sera or other liquids in the presence of other alkaline phosphatase isoenzymes.
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PMID:Alkaline phosphatase of human and calf small intestine. Purification and immunochemical characterization. 82 42

1. Alkaline phosphatase (orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1) from human intestine was purified with concanavalin A-Sepharose and tyraminyl derivative-Sepharose affinity chromatography. The enzyme obtained with these techniques had a specific activity of approx. 513.2 mumol p-nitrophenylphosphate hydrolyzed per min per mg of protein at pH 10.0. 2. The highly purified enzyme showed one major enzymatically active band and a possible minor enzymatically active band on acrylamide gel and cellogel electrophoresis, and the two fraction types showed identical antigenicity. 3. The highly purified intestinal enzyme was compared with the purified hepatic enzyme: the saccharide content of each showed a marked difference. 4. The interaction of alkaline phosphatase with concanavalin A, a carbohydrate-binding protein, was studied. Concanavalin A showed an organ-specific behavior to alkaline phosphatase isoenzyme, i.e., the effect on the enzyme activity, and the optimum pH of the activity. 5. The concanavalin A and alkaline phosphatase complex showed a protective effect against heat denaturation and inactivation of proteinase digestion. There was no difference in stability between the intestinal enzyme and the hepatic enzyme. 6. Alkaline phosphatase preparations from human intestine and human liver can bind with concanavalin A; these interactions of concanavalin A; these interactions of concanavalin A with the enzyme occurred reversibly when alpha-methyl-D-mannoside was added. 7. The double reciprocal plots of 1/v vs. 1/s at higher concentrations of concanavalin A showed that the mechanism of inhibition was "mixed type". From the results of Dixon plots, the inhibition constant (Ki) was calculated to the 0.025 muM for human intestinal enzyme. 8. The effect of concanavalin A on L-phenylalanine inhibition of the intestinal alkaline phosphatase indicates that concanavalin A does not interfere with L-phenylalanine binding, but its effect on L-homoarginine inhibition of the hepatic enzyme seems to show that concanavalin A interfered with L-homoarginine binding.
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PMID:Partial purification of human intestinal alkaline phosphatase with affinity chromotography. Some properties and interaction of concanavalin A with alkaline phosphatase. 82 66

Liver, intestinal, and bone alkaline phosphatase isoenzymes were measured using heat stability and L-phenylalanine inhibition techniques in 78 patients on intermittent haemodialysis. Fifty-five patients had abnormalities in one or more of the isoenzymes. Changes in bone and intestinal alkaline phosphatase activities seemed to be related and raised liver isoenzyme activity was associated with the development of liver disease. Abnormal histological and radiological findings were better correlated with bone alkaline phosphatase levels than with total alkaline phosphatase, and serial estimations of bone isoenzyme activity were useful in assessing the response of renal osteodystrophy to treatment with a vitamin D analogue. Serum alkaline phosphatase isoenzyme measurement provides another useful and non-invasive index for monitoring metabolic bone disease in patients with chronic renal failure.
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PMID:Comparative study of alkaline phosphatase isoenzymes, bone histology, and skeletal radiography in dialysis bone disease. 86 92


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