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)

Blood samples were taken before and immediately after 80 km and 40 km rides held on consecutive days and analysed for haematocrit, blood glucose and lactate, plasma sodium, potassium, calcium, albumin, free fatty acids (FFA), glycerol, bicarbonate, insulin, cortisol, glucagon, urea, creatinine, uric acid, bilirubin and alkaline phosphatase. Unusually hot weather probably contributed to haemoconcentration with a significant (P < 0.001) increase in haematocrit and plasma albumin. A fall in blood glucose, with a rise in FFA and glycerol were consistent with long distance riding and were associated with a reduction in plasma insulin and a rise in cortisol and glucagon. The results suggested that the horses were working aerobically and the small increase in blood lactate was likely to be a result of reduced tissue perfusion. Plasma urea, creatinine and bilirubin increased during the 80 km ride and were still high the next morning. Blood samples were taken from 2 horses that became exhausted and were forced to retire and the results from these animals indicate the slow rate of recovery. It is suggested that haemoconcentration with reduced tissue perfusion might contribute to exhaustion during long distance exercise and that the speed of recovery might be improved by the intravenous administration of balanced electrolyte solutions.
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PMID:Further studies on the metabolic effects of long distance riding: Golden Horseshoe Ride 1979. 743 43

In a comparative study, the differences between the values measured for 26 blood and serum components in both winter and summer were determined in 78 healthy subjects. Comparable conditions during the preparation of test persons, sampling, processing of specimens, and measurement were strictly observed. The term "season" is defined more precisely by meterological data. In the summer season, significantly higher values were found for leukocytes (9%), lactate dehydrogenase and MCHC (7% each), creatinine (7%, in women only), and MCH (1%) whereas significantly lower values were exhibited by aspartate aminotransferase (18%), alanine aminotransferase (14%), alkaline phosphatase (11%), glucose and packed cell volume (7% each), MCV (6%), total protein (2%), erythrocytes, albumin, sodium and chloride (1% each). These partly considerable alterations should be taken into account in the establishment of reference values and evaluation of laboratory findings (above all, when intraindividual comparison is involved). There were no significant alterations of the following parameters: hemoglobin, gamma-glutamyl transferase, urea, uric acid, creatinine (men only), bilirubin, cholesterol, total glycerol, potassium, calcium, and inorganic phosphate. In another series of experiments involving 32 test persons, the influence of different ambient temperatures during blood sampling on the above mentioned blood components was studied. Within the 18-30 degrees C range, no significant alterations were detected.
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PMID:[Seasonal variation of blood components important for diagnosis (author's transl)]. 744 84

Blood samples were taken before and after a cross country race over the marathon distance of 42 km. There was a rise in blood glucose and plasma free fatty acids and glycerol associated with a rise in plasma cortisol and glucagon but the fall in insulin was not significant (P > 0.05). Plasma potassium and albumin concentrations increased, calcium decreased and there was no change in sodium or bicarbonate concentrations. There was an increase in plasma urea, creatinine, uric acid, bilirubin and isocitrate dehydrogenase but no change in alkaline phosphatase. There was a rise in plasma creatine kinase. These results of a competitive race are compared with those of the 80 km non-competitive Golden Horseshoe Ride.
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PMID:A biochemical study of the Arab Horse Society's marathon race. 746 99

Snake venom phosphodiesterase (SVP) catalyzes the alcoholysis of ATP by primary R-CH2OH alcohols with uncharged R residues, yielding AMP-O-CH2R esterification products. The alcohols compete with water for an SVP-bound adenylyl intermediate. In this study, it has been shown that SVP also catalyzes the reactions of glycerol 2-phosphate and sn-glycerol 3-phosphate with ATP to yield AMP-O-glycerophosphoryl esters. The products were identified by HPLC, the dependency of the reactions on glycerol phosphates, ultraviolet spectroscopy, and conversion to AMP by phosphodiesterase, or to AMP-O-glyceryl esters by alkaline phosphatase. The results demonstrated that R-CH2OH alcohols with negatively charged R residues, as well as secondary alcohols, act as adenylyl acceptors in SVP reactions, thus extending the usefulness of SVP as a tool to produce 5'-nucleotide derivatives. The efficiencies (EA) of glycerol phosphates as adenylyl acceptors were very high at low, millimolar concentrations, but decreased abruptly when the acceptor concentration was increased and, for glycerol 2-phosphate, when Pi or NaCl was present. In contrast, glycerol EA was independent of its own concentration, Pi, and NaCl. The responses of glycerol phosphates indicate that they act as adenylyl acceptors via a mechanism different from uncharged R-CH2OH alcohols. The occurrence of an acceptor-binding enzyme site, specific for negatively charged R residues, and its potential relevance to the in vivo role of 5'-nucleotide phosphodiesterases as 5'-nucleotidyl transferases are discussed.
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PMID:High efficiency of glycerol 2-phosphate and sn-glycerol 3-phosphate as nucleotidyl acceptors in snake venom phosphodiesterase esterifications. Formation of primary and secondary AMP-O-glyceryl and AMP-O-glycerophosphoryl esters and evidence for an acceptor-binding enzyme site. 758 86

The multicomponent solution, containing 15% of glycerol, 4.5% of proteins, 0.9% of sodium chloride, 0.33% of potassium chloride and water for injections, was proposed. The ferments activity (aminotransferases, cholinesterase, aldolase, alkaline phosphatase), blood coagulating system state (the prothrombin level, plasma tolerance, her recalcification time), the mineral elements contents (potassium, sodium, calcium), the contents of protein and its fractions in blood before and after an acute blood loss compensation with the multicomponent solution, and also its influence on the animals organism in prolonged daily (during 30 days) intravenous injection were studied. The combination of components in the solution permit to store the studying indexes on level close to initial; if the loss of blood compensates in the first hours, high survival of animals is insured. Negative reactions of organism while prolonged intravenous injection of the multicomponent solution are not revealed.
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PMID:[Use of glycerin as a component of the solution in treating acute hemorrhage]. 760 2

The hybridization characteristics of oligonucleotide-alkaline phosphatase conjugate probes were examined in bead-based sandwich hybridization reactions using single-stranded nucleic acid targets and oligonucleotide-polystyrene capture beads. Enzymatic activity was monitored using a chemiluminescent substrate and calibration plots of chemiluminescent signal versus conjugate concentration were used to estimate the sandwich hybridization efficiencies. Improved hybridization behavior was noted using glycerol as an additive and by increasing the length of the probe and alkyl spacer of the conjugates. The chemiluminescent assay is at least as sensitive as those employing 32P-labeled probes and can detect as little as 10-20 amol of target RNA. The linear relationship of chemiluminescent signal versus target assayed provides a method for quantitating unknown target samples. A single human immunodeficiency virus type 1 infected cell in a background of 10(6) uninfected cells is facilely detected when this enzyme-based detection assay is prefaced with a self-sustained sequence-replication amplification reaction.
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PMID:Bead-based sandwich hybridization characteristics of oligonucleotide-alkaline phosphatase conjugates and their potential for quantitating target RNA sequences. 767 91

The hydrolysis and transphosphorylation reactions of a series of phosphate monoesters, ROPO3(2)-(R = 2,4-dinitrophenyl, 4-nitrophenyl, phenyl, glucose-1, glycerol-1, methyl, ethyl, and dodecyl), catalyzed by Escherichia coli alkaline phosphatase and a mutant enzyme, Ser102Cys, have been studied at alkaline pH using the rates of change in the 31P NMR signals of substrate, the hydrolysis product (inorganic phosphate), and the transphosphorylation product (O-Tris phosphate) as the assay. The kcat at pH 8.0 for the wild-type enzyme is approximately 30 s-1 and is independent of the nature of the R group, when the pKa of the leaving group is < 10. Under these conditions the rate of phosphorylation is much faster than dissociation of inorganic phosphate, 15-60 s-1. If the pKa of the leaving group is between 10 and 15, phosphorylation and dissociation of the product phosphate both contribute to the rate limit. If the pKa of the leaving group is > 15, phosphorylation is rate limiting. A Bronsted plot of log kcat vs pKa of the leaving group for those substrates for which phosphorylation is rate limiting yields a beta lg of approximately -0.6. In contrast to the wild-type enzyme, the log kcat values for the S102C mutant enzyme catalyzing the hydrolysis of phosphate esters are linearly dependent on the pKa's of the leaving group throughout the range of pKa from 4 to 16. Phosphorylation of C102 is the rate controlling step, and kcat is independent of the Tris concentration as predicted for rate limiting phosphorylation.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Dependence of the phosphorylation of alkaline phosphatase by phosphate monoesters on the pKa of the leaving group. 770 37

The chemiluminescent reaction of lucigenin with various reducing sugars and reducing compounds has been studied. It was found that dihydroxyacetone gave the most intense chemiluminescence (CL). We have developed highly sensitive chemiluminescent methods for alkaline phosphatase (ALP) based on the production of dihydroxyacetone using NADP+ or glycerol-3-phosphate as substrate. The detection limits for ALP using each substrate were 1.25 x 10(-19) mol/assay and 2.5 x 10(-19) mol/assay, and the coefficient of variation (n = 7) was 2.8% and 3.7%, respectively. We have also applied the method using NADP+ as substrate in enzyme immunoassays (EIA) for cholecystokinin (CCK) and human chorionic gonadotropin (hCG). CCK-8 (octapeptide sulphated form of a carboxy terminal fragment of CCK) concentrations released from alimentary canal of rat were assayed using the chemiluminescent EIA (CLEIA) and a fluorimetric EIA (ALP label). The correlation between CCK-8 values obtained by these methods was y = 1.04x + 18.21, r = 0.946, n = 28. hCG values in serum and in urine were measured. The correlation between hCG values in serum samples obtained using the CLEIA and a time-resolved fluoroimmunoassay (TR-FIA), and in urine samples obtained using the CLEIA and the fluorimetric EIA using ALP were satisfactory. The correlations were y = 1.00x - 0.04, r = 0.997 (n = 51) and y = 1.00x - 0.03, r = 0.999 (n = 10), respectively.
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PMID:A new highly sensitive chemiluminescent assay of alkaline phosphatase using lucigenin and its application to enzyme immunoassay. 776 11

Lung surfactant was isolated from human amniotic fluid collected at term and studied with reference to the material isolated from human and rabbit lung lavage. The isolated material showed 58 per cent lipid by dry weight, 29 per cent protein and relatively smaller amounts of nucleic acids, sialic acid and hexose. Phosphatidyl choline was the predominant phospholipid species and accounted for 46 per cent of the total lipid by weight, followed by phosphatidyl glycerol (7%) and phosphatidyl ethanolamine (5%). Cholesterol was the major neutral lipid fraction present (10%) and was almost entirely in the free form. Other lipid fractions present in minor quantity were triglycerides, esterified cholesterol, phosphatidyl serine, phosphatidyl inositol and sphingomyelin. The material contained a very high degree of alkaline phosphatase activity, while other enzymes such as acid phosphatase, glucose-6-phosphatase, ATPases, 5'-nucleotidase and beta-N-acetyl glucosaminidase were also present.
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PMID:Isolation & chemical composition of lung surfactant from human amniotic fluid. 800 43

The second-order rate constant, kcat/km, for catalysis of the hydrolysis of 4-nitrophenyl phosphate by alkaline phosphatase decreases with increasing viscosity in the presence of sucrose or arabinose, with a slope of delta[kcat/Km)0/(kcat/Km)]/delta(eta/eta 0) = 1.4 at pH 8.0, 25 degrees C. This is consistent with rate-limiting diffusional encounter of the substrate with active enzyme and indicates that alkaline phosphatase is a "perfect enzyme". However, the reported second-order rate constants of kcat/Km = 6.6 x 10(6) to 4.6 x 10(7) M-1 s-1 are smaller than the diffusional limit; this shows that only approximately 0.1-1% of the diffusional encounters are productive. The first-order rate constant, kcat, for rate-limiting hydrolysis of the phosphoenzyme intermediate at pH = 6 with saturating substrate concentration is independent of viscosity in aqueous sucrose solutions. This shows that sucrose does not destabilize the transition state for phosphoenzyme hydrolysis. However, at pH 8.0 product dissociation is rate limiting and kcat decreases with increasing viscosity in the presence of sucrose, with slopes of delta(k0/kobsd)/delta(eta/eta 0) = 1.2 in 0.04 M Mops buffer, 1.0 in 0.1 M Tris, and 1.2 in 0.67 M Tris buffer. This is consistent with rate-limiting diffusional separation of inorganic phosphate and of Tris phosphate from the enzyme. In contrast, glycerol causes a large decrease in kcat/Km at pH 8.0 and also decreases kcat at pH 6. This shows that glycerol decreases the rate by a solvent effect on the catalytic activity of the enzyme, as well as by increasing the viscosity.
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PMID:Alkaline phosphatase is an almost perfect enzyme. 806 74


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