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)

The placement of rubber band tourniquets upon rat hind-limbs for 5 h followed by reperfusion of the extremities results in a severe form of circulatory shock characterized by hypotension and death within 24 h of tourniquet release. Oxidative damage to muscle tissue is an early consequence of hind-limb reperfusion on tourniquet release, yet this local damage does not explain the lethal hypotensive shock state which evolves within the next 24 h. Multiple system organ failure (MSOF), of as of yet unknown causes, is usually described in relation to several shock states. It has been suggested that injured or necrotic tissue may activate neutrophils, platelets, and the coagulation system leading to embolization in remote tissues. Effective decreases in hepatic blood flow have been observed in several forms of sepsis which precedes the biochemical evidence consistent with an ischemic insult of the liver. In support of our original hypothesis, that organ failure has its genesis in a primary perfusion abnormality with secondary ischemic organ injury, herein we have assessed the possibility that oxygen-derived free radicals are generated in the liver of rats after reperfusion of their hind-limbs on release of the tourniquets. We report on the protective effects of allopurinol (ALLO) and a mixture of superoxide dismutase (SOD) catalase (CAT) and dimethylsulfoxide (DMSO) on liver free sulfhydryl content (SH), thiobarbituric acid-reactive substances (TBARS), and on the release of aspartic acid (AsT) and alanine aminotransferase (AlT) activities, and of alkaline phosphatase during a 5 h tourniquet period and after 2 h of reperfusion of the hind-limbs. During the hind-limb ischemic period hepatis tissue SH levels remained essentially constant during the first hour (6.02 +/- 0.36 to 5.65 +/- 0.20 mumoles/g wet tissue), and decreased significantly, over and above the normal circadian decrease of liver glutathione levels, to 4.02 +/- 0.69 mumoles/g wet tissue after the third hour and remained lowered until tourniquet release. A further significant decrease (3.11 +/- 0.49 mumoles/g wet tissue) was observed after 2h of reperfusion. TBARS production remained constant during the 5 h hind-limb ischemic period (168.4 +/- 37.3 mumoles/g wet tissue) and rose by 55% to 261.7 +/- 55.8 mumoles/g wet tissue after 2 h of tourniquet release. ALLO, but not the SOD-CAT-DMSO combination, protected hepatic SH loss during the hind-limb ischemic insult, yet both offered protection after 2 h of tourniquet release.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Oxygen-derived free radicals mediate liver damage in rats subjected to tourniquet shock. 148 82

49 women of reproductive age were included in the study and were divided in 2 groups. The ovulation inhibitor group (OI) consisted of 37 women aged 33.5-39 exposed to ovulation inhibitors for an average of 13.4 years (Ovosiston, Sequenzovosiston, Non-Ovlon), and the control group consisted of 12 women aged 35.5-41.5 who had taken no OI for at least 5 years. Aspartate-aminotransferase (serum glutamic oxaloacetic transaminase=SGOT) and alanine aminotransferase (serum glutamic pyruvic transaminase) enzymes were determined as indicators of liver damage, and gamma-glutamyl-transferase (gamma-GT) for indication of cholestasis or as a sensitive parameter of hepatopathy. By using a nonradiating, stabile isotop-marked tracer substance, 15 N-ammonium chloride, the uric acid synthesis performance and the ammonium excretion of the liver could be evaluated. The Q-value indicated an excess of ammonium and uric acid as demonstrated by the 15 N test. Significant differences were found between the 2 groups with regard to ALAT, gamma-GT, Q-value, and leukocyte count. The measured values of enzymes and leukocytes studied, however, stayed within the normal range. In the OI group, the decreased gamma-GT activity was surprising. Also, the Q-value showed a slightly pathological median value in 18 women of the OI group. In 4 women who has Q-values of 1.6 to 1.9 (vs. 1.4 median value), liver punction was performed. In each case, liver damage could be shown to be attributed to use of contraceptives. Morphological changes indicating enhanced detoxification activity, and liver cell fat formation of various severity were also found as uncharacteristic alterations. The described increase of the serum activity of aminotransferase, leucine aminopeptidase, alkaline phosphatase, and gamma-GT were interpreted as the expression of cellular adaptation. Long-term use of hormonal contraceptives influences the metabolism of the liver, whose partial disorder can be detected by the 15 N-ammonium test. Normal ALAT and gamma-GT serum enzyme activity in single cases does not allow conclusions on the behavior of the metabolism of the liver.
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PMID:[Use of the stable nitrogen isotope 15N in assessing liver metabolism in hormonal contraception]. 231 86

We examined the cytoprotective action of individual amino acids in isolated perfused kidneys during perfusion with either 10 mM lactate or 5 mM glucose. In the absence of amino acids inulin clearance fell rapidly, whereas fractional excretion of phosphate, lactate, or glucose increased to more than 30%; lactate dehydrogenase was released into perfusate and alkaline phosphatase into the urine. Functional deterioration was less in kidneys from rats rendered chronically water diuretic by drinking 5% glucose. Adding 5 mM glycine, L-alanine, beta-alanine, or D-alanine to the perfusate also prevented functional deterioration and release of enzymes. Glycine perfusion increased total phospholipid per microgram DNA by 6%. Aspartate, glutamate, glutamine, taurine, isoleucine, leucine, and valine were not protective. Serine, proline, and alpha-aminoisobutyric acid had small protective effects. Micropuncture measurements of proximal tubular free- and stop-flow pressures showed no effect of L-alanine on glomerular hemodynamics. L-Alanine increased oxygen consumption by both glucose- and lactate-perfused kidneys and increased gluconeogenesis by lactate-perfused kidneys but did not alter renal ATP content or energy charge. L-Alanine was not consumed during 70 min of perfusion and its protective action was not inhibited by blocking transamination with 0.5 mM amino-oxyacetate. The protective action of glycine was not inhibited by blocking glycine metabolism with 0.1 mM cysteamine. Thus the beneficial effects of L-alanine and glycine do not require their metabolism. These observations suggest that small neutral amino acids prevent tubular disruption through their physicochemical effects, which can stabilize membrane protein tertiary structure.
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PMID:Mechanisms of perfused kidney cytoprotection by alanine and glycine. 237 94

The function of aspartic acid residue 101 in the active site of Escherichia coli alkaline phosphatase was investigated by site-specific mutagenesis. A mutant version of alkaline phosphatase was constructed with alanine in place of aspartic acid at position 101. When kinetic measurements are carried out in the presence of a phosphate acceptor, 1.0 M Tris, pH 8.0, both the kcat and the Km for the mutant enzyme increase by approximately 2-fold, resulting in almost no change in the kcat/Km ratio. Under conditions of no external phosphate acceptor and pH 8.0, both the kcat and the Km for the mutant enzyme decrease by approximately 2-fold, again resulting in almost no change in the kcat/Km ratio. The kcat for the hydrolysis of 4-methyl-umbelliferyl phosphate and p-nitrophenyl phosphate are nearly identical for both the wild-type and mutant enzymes, as is the Ki for inorganic phosphate. The replacement of aspartic acid 101 by alanine does have a significant effect on the activity of the enzyme as a function of pH, especially in the presence of a phosphate acceptor. At pH 9.4 the mutant enzyme exhibits 3-fold higher activity than the wild-type. The mutant enzyme also exhibits a substantial decrease in thermal stability: it is half inactivated by treatment at 49 degrees C for 15 min compared to 71 degrees C for the wild-type enzyme. The data reported here suggest that this amino acid substitution alters the rates of steps after the formation of the phospho-enzyme intermediate.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Alteration of aspartate 101 in the active site of Escherichia coli alkaline phosphatase enhances the catalytic activity. 268 45

The effects of the progestational compound dienogest (17 alpha-cyanomethyl-17 beta-hydroxy-estra-4,9-dien-3-one) on liver metabolism have been studied in 101 otherwise healthy women with endoscopically proven endometriosis. The women aged 17 to 45 years were treated with 2 mg dienogest in tablet form daily for 24 weeks. Aspartate amino transferase (ASAT), alanine amino transferase (ALAT), gamma glutamate transferase (GGT), alkaline phosphatase (AP), lactate dehydrogenase (LDH), and total bilirubin (BILI) were determined in serum before and after 1, 3 and 6 months use of the progestin. During the therapy period no deviations from the normal ranges were found. There was a slight significant decrease of ASAT and ALAT and a slight significant increase of LDH and BILI (p less than 0.05) remaining within the normal laboratory values. Since no undesirable metabolic side-effects have so far been observed with dienogest, it may be considered an effective new alternative treatment for endometriosis.
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PMID:[Behavior of parameters of liver metabolism in intermediate-term use of the gestagen dienogest in the treatment of endometriosis]. 276 50

The nucleotide sequence of the alkaline phosphatase (APase) gene (phoA) of Escherichia coli strain 294 has been determined. Pre-APase has a total of 471 amino acids (aa) including a signal sequence of 21 aa. The derived aa sequence differs from that obtained by protein sequencing by the presence of aspartic acid instead of asparagine at positions 16 and 36, and glutamic acid instead of glutamine at position 197. Two open reading frames (ORF1 and ORF2) located downstream from phoA or upstream from proC have been found. ORF1 encodes a putative presecretory protein of 106 aa with a signal sequence of 21 or 22 aa. If this protein is actually produced, it may be one of the smallest periplasmic proteins in E. coli.
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PMID:Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli. 353 24

Different patterns of isozymes were obtained by starch-gel electrophoresis of alkaline phosphatase from Escherichia coli strains differing only by strA or ram mutations, or both, in the 30S ribosomal subunit. The isozyme spread was reduced in strA and increased in ram strains; this strictly parallels the restriction and enhancement of translational ambiguity produced by these mutations. Streptomycin present during growth had an effect similar to ram on both isozymes and ambiguity. The three isozymes analyzed have different N-terminal residues: aspartic acid, valine, and threonine. Different patterns of isozymes were also obtained in a wild-type strain through the specific action of exogenous arginine. A link between the mechanism of the effect of arginine and that of the ribosome is not obvious. The possibility is discussed that in both cases, although by different mechanisms, N-terminals are formed with different sensitivity to limited degradative attack.
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PMID:Ribosomal alterations controlling alkaline phosphatase isozymes in Escherichia coli. 455 93

1. Acid phosphatase (AcPase) from potato tubers was purified by tannic acid fractionation, DEAE-cellulose chromatography, filtration on Bio-Gel P-150 and affinity chromatography on Con A-Sepharose. The enzyme was purified 260-fold and was electrophoretically homogeneous; its mol. mass is about 69 000. 2. The carbohydrate component accounts for 16.6% of the total enzyme weight and includes mannose (5.6%), rhamnose (3.4%), glucose (2.5%), galactose (1.5%) and glucosamine (3.6%). In the amino acid composition aspartic acid, glutamic acid, serine and glycine account for 37.7% of total amino acid residues. 3. Optimum pH is at 5.0-5.3. The enzyme activity was reduced by half after 30 min incubation at 60 degrees C, and was fully abolished after 2 h incubation at 70 degrees C. The enzyme is a nonspecific phosphomonoesterase; aromatic phosphomonoesters and inorganic pyrophosphate can serve as substrates. Apparent Km values were 1.25 mM and 40 mM for p-nitrophenylphosphate and inorganic pyrophosphate, respectively. The enzyme is inhibited by MoO42-, Zn2+, Hg2+ and urea. Inhibition caused by urea was reversible at urea concentration below 9 M.
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PMID:Acid phosphatase of potato tubers (Solanum tuberosum L). Purification, properties, sugar and amino acid composition. 715 77

Three high-performance cows in lactation were tested each for the effects of two kinds of infusion each, 500 ml of Tetamag-2 solution (60 g of calcium gluconate and 60 g of magnesium adipate) and 500 ml of Calcimag (100 g of calcium gluconate and 20 g of magnesium adipate), upon the levels of calcium, magnesium, Pa, potassium, and sodium as well as upon the activities of aspartate-aminotransferase, leucine-aminopeptidase, and alkaline phosphatase in blood serum and upon glucose levels in blood plasma. Migration of calcium out of blood plasma was found to take place at much higher rate than that of magnesium. Infusion of Pa and glucose was followed soon by some temporary drop of values. No directional effects were recordable from potassium and sodium. Aspartate-aminotransferase activity did not change in response to transfusion. Intravenous infusion of Tetamag-2 solution caused strong temporary rise in magnesium concentration and, consequently, activation of leucine-aminopeptidase.
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PMID:[Modification of blood serum mineral levels and aspartate aminotransferase, leucine aminopeptidase and alkaline phosphatase activity and plasma in glucose levels in healthy cattle by Ca-Mg-containing solutions]. 722 93

The levels of various compounds in blood serum and blood plasma were tested in 14 heads of cattle with hypomagnesiaemia (x = 0.76 +/- 0.29 mg/100 ml), prior to and following infusion of 500 ml of a calcium-magnesium solution (containing 60 g of magnesium adipate and 60 g of calcium gluconate). Concomitant hypocalcaemia (6.1 mg/100 ml) was recordable only from one animal. Most of the potassium as well as all Pa and protein values in blood serum were physiologically normal, while sodium ws somewhat reduced. The glucose level in blood plasma was increased in the animal with concomitant hypocalcaemia and in one animal with poor recovery potential. The drops in magnesium and calcium levels in blood serum, following infusion, in cattle with hypomagnesiaemia was very similar to that in clinically intact cattle. Aspartate-aminotransferase and creatinine-phosphokinase activities of the serum were increased in all cattle, but leucine-aminopeptidase activity in only some of them. The activity of alkaline phosphatase of the blood serum was physiologically normal.
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PMID:[Blood mineral (Ca, Mg, Na K, Pa) levels and aspartate aminotransferase, leucine aminopeptidase, creatine phosphokinase and alkaline phosphatase activity and blood glucose levels in cattle with hypomagnesemia prior to and following infusion of a 500 ml solution containing 60 g of Mg adipate and 60 g of Ca gluconate]. 722 94


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