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)

Elevated levels of serum enzymes are frequently associated not only with alcohol-related organ damage but also with excessive alcohol consumption and alcoholism without significant tissue injury. However, both in the early detection of alcoholism as well as also in the diagnosis of alcohol-related diseases the sensitivities and specificities of these enzyme markers vary considerably. They may be influenced by nonalcohol-related diseases, enzyme-inducing drugs, nutritional factors, metabolic disorders, age, smoking, etc. Consequently, we have neither a single laboratory test--enzyme marker--nor a test combination that is reliable enough for the exact diagnosis between alcohol- and nonalcohol-related organ damage. In most cases it is possible to determine the tissue from which the elevated enzyme is derived, but only occasionally enzyme changes reflect the quantity of the tissue injury. Gamma-glutamyltransferase (GGT) is the most widely used laboratory marker of alcoholism and heavy drinking, detecting 34-85% of problem drinkers and alcoholics. However, the unspecificity of increased serum GGT limits its use for general screening purposes. Its value in the follow-up of various treatment programs, however, is well established. An elevated level of serum aspartate aminotransferase (ASAT) and alanine aminotransferase (ALAT) in an alcoholic or a heavy consumer indicates alcohol-induced organ damage. The use of test combinations significantly improves the information received with single serum enzyme determinations. An ASAT/ALAT ratio greater than 1.5 can be considered as highly suggestive for the alcoholic etiology of the liver injury. Still better discrimination between alcoholic and nonalcoholic origin of the liver disease may be achieved by the determination of the ratio of GGT to alkaline phosphatase. If this ratio exceeds 1.4 the specificity of the finding in favor for alcoholic liver injury is 78%. The determination of the mitochondrial isoenzyme of ASAT also improves the diagnostic value of ASAT determination. The ratio of mitochondrial isoenzyme to total over 4 is highly suggestive for alcohol-related liver injury. In general, however, the determination of serum activities of other enzymes such as ornithine carbamyl transferase, lactate dehydrogenase, isocitrate dehydrogenase, sorbitol dehydrogenase, alcohol dehydrogenase, guanase, aldolase, alkaline phosphatase or glutathione S-transferase do not significantly improve the diagnostic information obtained with more conventional laboratory markers of liver injury.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Use of enzymes for the diagnosis of alcohol-related organ damage. 243 6

The interaction of alpha-chymotrypsin, invertase, alcohol dehydrogenase and alkaline phosphatase with some ionic and non-ionic surfactants, viz. sodium dodecyl sulphate, dioctyl sodium sulphosuccinate, hexadecyltrimethylammonium bromide, tetradecyltrimethylammonium bromide and Triton X-100, has been examined by studying the effect of varying surfactant concentrations on enzyme activities as well as by determining the time-dependent inactivation and the time-independent inhibition. The kinetic parameters, Km and Vmax, for alpha-chymotrypsin-catalysed reaction in presence of sodium dodecyl sulphate were evaluated. Anionic surfactants markedly decreased enzyme activity, whereas cationic surfactants were less effective. Nonionics showed no effect. This change in enzyme activity was also dependent on the nature of enzyme.
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PMID:Stability and kinetic behaviour of some enzymes in surfactant environment. 263 63

A simple chemical method for introducing biotin into nucleic acids has been developed for the synthesis of nonisotopic hybridization probes. The method is based on the reaction of biotin hydrazide with amino residues of nucleic acids by using glutaraldehyde as a bifunctional coupling reagent. Biotin-labelled deoxyribonucleic acid (DNA) was detected by the use of alkaline phosphatase-labelled avidin, and alkaline phosphatase activity was measured by colorimetric and chemiluminescence methods. The chemiluminescence method using the nicotinamide adenine dinucleotide phosphate (NADP)/alcohol/alcohol dehydrogenase/microperoxidase/isoluminol system gave the highest sensitivity. A few picograms of lambda-phage DNA coated on a microtiter plate well could be detected by this method.
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PMID:Highly sensitive biotin-labelled hybridization probe. 280 62

We have previously reported the detection of a 37 kD liver protein-acetaldehyde adduct in rats fed alcohol chronically with the AIN'76 diet. It was surprising that only one liver protein-acetaldehyde adduct was found. In this report, we have tried to detect additional protein-acetaldehyde adducts by electroimmunotransblot with rabbit anti-hemocyanin-acetaldehyde adduct IgG and to further characterize the 37 kD liver protein-acetaldehyde adduct. Sensitivity of electroimmunotransblot increased 10- to 20-fold when alkaline phosphatase-linked antibody was used in place of horseradish peroxidase, but only one protein-acetaldehyde adduct band was detected in liver. Feeding rats the Lieber-DeCarli alcohol diet also did not produce more protein-acetaldehyde adduct bands in electroimmunotransblot. Addition of cyanamide, an aldehyde dehydrogenase inhibitor, to the AIN'76 alcohol diet greatly increased the intensity of the 37-kD protein-acetaldehyde adduct band on electroimmunotransblot but did not produce other bands. The 37 kD protein-acetaldehyde adduct decayed in vivo with a half-life of 4 days when alcohol was removed from the diet. The 37 kD protein-acetaldehyde adduct in liver is cytosolic. Its interaction with anti-hemocyanin-acetaldehyde adduct IgG was blocked by polylysine-acetaldehyde adduct and polytyrosine-acetaldehyde adduct. It could be removed by immunosorption with anti-hemocyanin-acetaldehyde adduct IgG-bound immunoresin. When immunoblotted with anti-alcohol dehydrogenase and anti-aldehyde dehydrogenase antibodies, the alcohol dehydrogenase and aldehyde dehydrogenase bands in liver of alcohol-fed rats showed identical intensities before and after immunosorption.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Further studies on the 37 kD liver protein-acetaldehyde adduct that forms in vivo during chronic alcohol ingestion. 280 59

A number of molecular agents that can efficiently quench the room temperature phosphorescence of tryptophan were identified, and their ability to quench the phosphorescence lifetime of tryptophan in nine proteins was examined. For all quenchers, the quenching efficiency generally follows the same sequence, namely, N-acetyltryptophanamide (NATA) greater than parvalbumin approximately lactoglobulin approximately ribonuclease T1 greater than liver alcohol dehydrogenase greater than aldolase greater than Pronase approximately edestin greater than azurin greater than alkaline phosphatase. Quenching rate constants for O2 and CO are relatively insensitive to protein differences, while H2S and CS2 are somewhat more sensitive. These small molecule agents appear to act by penetrating into the proteins. However, penetration to truly buried tryptophans is less favorable than previously suggested; in five proteins studied, quenching efficiency by O2 is 20-1000 times lower than for NATA, and up to 10(5) lower for H2S and CS2. Larger and more polar quenchers--including organic thiols, conjugated ketones and amides, and anionic species--were also studied. The efficiency of these quenchers does not correlate with quencher size or polarity, the quenching reaction has low energy of activation, and quenching rates are insensitive to solvent viscosity. These results indicate that the larger quenchers do not approach the buried tryptophans by penetrating into the proteins, even on the long phosphorescence time scale, and are also inconsistent with a mechanism in which quencher encounter with the tryptophan occurs in free solution, as in a protein-opening reaction. The results obtained suggest that the quenching process involves a long-range radiationless transfer.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Quenching of room temperature protein phosphorescence by added small molecules. 324 96

A method is described for increasing the response of enzyme immunoassays employing alkaline phosphatase as the label initiating 2 sequential catalytic reactions. First, NADP is dephosphorylated to produce NAD, which catalytically activates a specific redox-cycle involving the enzymes alcohol dehydrogenase and diaphorase. During each turn of the cycle 1 molecule of a tetrazolium salt is reduced to an intensely coloured formazan. The method is capable of detecting as little as 0.01 amol alkaline phosphatase, and when applied to an immunoassay for TSH a sensitivity (zero + 2.5 standard deviations) of 0.0013 mIU/l was obtained.
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PMID:Enzyme amplification for immunoassays. Detection limit of one hundredth of an attomole. 351 23

The influence of chelating agents (1 mmol/kg/day X 6,i.p.) on trace metal mobilization and activities of certain metalloenzymes was investigated in rats. Calcium disodium ethylenediamine tetraacetate (CaNa2EDTA) and calcium trisodium diethylenetriamine pentaacetate (CaNa3DTPA) enhanced urinary excretion of Zn, while sodium 2,3-dimercaptopropane-1-sulfonate (NaDMPS) and sodium diethyldithiocarbamate (NaDDC) increased that of Cu. The activity of Zn-metalloenzymes-blood delta-aminolevulinic acid dehydratase (delta-ALA-D), plasma alkaline phosphatase (ALP) and that of Cu-metalloenzyme-plasma amine oxidase was decreased as a consequence of chelation therapy. However, hepatic levels of delta-ALA-D, ALP and alcohol dehydrogenase remained unaffected by chelation. The activity of hepatic Fe-metalloenzyme-catalase was increased by polyaminocarboxylic acids and lowered by thiol chelators. The metal chelators decreased the hepatic glutathione levels.
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PMID:Influence of metal chelators on metalloenzymes. 361 94

High levels of alkaline phosphatase and alcohol dehydrogenase were observed in the serum, liver and kidneys of rats fed on high sucrose and high alcohol diets over a period of 75 days. Garlic oil extract fed with any of the diets, significantly lowered the high levels of the two enzymes in the serum, liver and kidneys. This effect may be due to reduced biosynthesis of fatty acids as NADPH, required for the process, is utilised for the metabolism of the oil.
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PMID:Effect of garlic oil extract on serum, liver and kidney enzymes of rats fed on high sucrose and alcohol diets. 380 Oct 36

Benzoyl- and isopentenoyl phosphoric triamides (BPA and IPA) strongly inhibited urease activities from jack bean, soybean, watermelon seed, Proteus mirabilis, P. rettgeri, P. vulgaris, Mycobacterium smegmatis, and Ureaplasma urealyticum. Their I50 values (the final concentration causing 50% inhibition), independent of enzyme source, were 2-21 nM, which are about 1,000-fold lower than that of caprylohydroxamic acid, one of the most potent urease inhibitors. ATP-urea amidolyase activity was inhibited 50% by BPA at a higher concentration of 0.28 mM, but was not affected by IPA even at 1.3 mM. Thirteen kinds of hydrolases (trypsin, chymotrypsin, thermolysin, leucine aminopeptidase, papain, lipase, alpha-amylase, glucuronidase, asparaginase, arylsulfatase, alkaline phosphatase, acid phosphatase, and true cholinesterase), two oxidoreductases (catalase and alcohol dehydrogenase), three transferases (glutamic-oxaloacetic aminotransferase, gamma-glutamyl transpeptidase, and arylsulfotransferase) and two kinases (pyruvate kinase and creatine kinase) were not affected at all even at 1 mM BPA and IPA. Exceptionally, pseudo-cholinesterase from human serum was inhibited by BPA and IPA, whose I50 values were 70 nM and 10 muM, respectively, using acetylthiocholine as a substrate. These values increased to 0.55 muM and 54 muM, respectively, when acetylcholine was used as a substrate. These results show that N-acylphosphoric triamides potently and specifically inhibit urease activity at concentrations of nM order.
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PMID:Specific inhibition of urease by N-acylphosphoric triamides. 384 42

Zinc content of testes, bones, esophagus, kidneys, and muscles was decreased, whereas iron content was increased in the testes of zinc-deficient rats compared to restrictedly fed control rats. Histochemical enzyme determinations revealed reduced activities of certain enzymes in the testes, bones, esophagus, and kidneys. In the testes, lactic dehydrogenase (LDH), malic dehydrogenase (MDH), alcohol dehydrogenase (ADH), and NADH diaphorase; in the bones, LDH, MDH, ADH, and alkaline phosphatase; in the esophagus, MDH, ADH, and NADH diaphorase; and in the kidneys, MDH and alkaline phosphatase were decreased in zinc-deficient rats compared to restrictedly fed controls. Succinic dehydrogenase (SDH) revealed no significant changes under the conditions of our experiments in various groups of rats that were investigated. In a "repleted" group of rats, content of zinc in testes and bones increased significantly, compared to the deficient group. The iron content of the testes decreased after repletion with zinc. In the testes, bones, esophagus, and kidneys, the activities of various enzymes increased after repletion with zinc. Inasmuch as the major manifestations of zinc deficiency syndrome in the rat include growth retardation, testicular atrophy, and esophageal parakeratosis, our results suggest that the content of zinc in the above tissues most likely controls the physiological processes through the formation of zinc-dependent enzymes.
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PMID:Studies on zinc deficiency: changes in trace elements and enzyme activities in tissues of zinc-deficient rats. 429 21


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