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)

We have studied the phenotype and activation status of leukocytes in the bronchial mucosa in patients with isocyanate-induced asthma. Fiberoptic bronchial biopsy specimens were obtained from nine subjects with occupational (five toluene- and four methylene diisocyanate-sensitive) asthma, 10 subjects with extrinsic asthma, and 12 nonatopic healthy control subjects. Bronchial biopsy specimens were examined by immunohistology with a panel of monoclonal antibodies and the alkaline phosphatase-antialkaline phosphatase method. There was a significant increase in the number of CD25+ cells (interleukin-2 receptor-bearing cells, presumed "activated" T-lymphocytes; p less than 0.01) in isocyanate-induced asthma compared with that of control subjects. There were also significant increases in major basic protein (BMK-13)-positive (p less than 0.02) and EG2-positive (p less than 0.01) cells that represent total and "activated" eosinophil cationic protein-secreting eosinophils, respectively. In agreement with our previous findings, CD25+ (p less than 0.01), BMK-13 (p less than 0.03), and EG2+ (p less than 0.01) cells were also elevated in extrinsic asthma. No significant differences were observed in the numbers of T-lymphocyte phenotypic markers (CD3, CD4, and CD8) between subjects with asthma (isocyanate-induced and extrinsic) and control subjects. Similarly, no significant differences in immunostaining for neutrophil elastase (neutrophils) or CD68 (macrophages) were observed. The results suggest that isocyanate-induced occupational asthma and atopic (extrinsic) asthma have a similar pattern of inflammatory cell infiltrate. The results support the view that T-lymphocyte activation and eosinophil recruitment may be important in asthma of diverse etiology.
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PMID:Activated T-lymphocytes and eosinophils in the bronchial mucosa in isocyanate-induced asthma. 153 7

Several methods for the permeabilization of Saccharomyces cerevisiae M1 were compared. Cells were permeabilized in the presence of 3% toluene/mercaptoethanol, and the activities of 6-phosphofructo-2-kinase, fructose-2,6-bisphosphatase and alkaline phosphatase were measured during growth of yeast on glucose. In the exponential phase of growth, the specific activities of 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase decrease significantly. The specific activities of 6-phosphofructo-2-kinase and high-affinity fructose-2,6-bisphosphatase increase again during the transition phase and reach maximum values in the stationary phase. In contrast to the specific activities, the activity concentrations of 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase remain nearly constant in the exponential phase, but increase in the transition and the stationary growth phase. The concentration of fructose-2,6-bisphosphate drops from about 6 microM in the exponential phase to very low levels in the transition phase, but increases slightly in the stationary phase. In Saccharomyces cerevisiae M1 several fructose-2,6-bisphosphate degrading activities were measured differing in the behaviour during growth on glucose, in the pH-optimum and the inhibition by fructose-6-phosphate.
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PMID:Fructose-2,6-bisphosphate metabolism in permeabilized yeast cells. 166 44

Three techniques for visualization of alkaline phosphatase after polyacrylamide-gel electrophoresis are compared. These are diazo-dye simultaneous coupling with the substrate sodium naphthyl phosphate and 5-chloro-2-toluene diazonium chloride; formazan precipitation with the substrate 5-bromo-4-chloro-3-indolyl phosphate and 3-[4,5-dimethylthiazolyl-2)-2,5-diphenyltetrazolium bromide; and silver staining with the substrate sodium glycerophosphate. Each staining technique was tested with gradient-pore and homogeneous-pore acrylamide-gel electrophoresis. The main factors assessed are sensitivity; separation of the human serum alkaline phosphatase isoenzymes of the liver, bone, and intestinal types; and differences in substrate affinity, as well as the complexity of each technique. Using the three techniques only minor differences in substrate affinity are evident. There is some nonspecific staining with the diazo-coupling technique but not with the formazan and silver staining techniques. The differences, in the mobility of the liver, bone, and intestinal isoenzymes achieved by homogeneous-pore gel electrophoresis are sufficient to allow them to be clearly distinguished. However, only very small differences in mobility are found with gradient-pore gel electrophoresis, but the sharper bands in this medium allow much smaller amounts of activity to be detected. As little as 160 microU of enzyme can be visualized by the diazo technique. Silver staining gives an approximately fourfold increase in sensitivity over the formazan technique, which in turn gives a fourfold increase over the diazo technique. An important aspect of the silver staining technique is the potential of increasing sensitivity much further by improvements in the photographic physical development stage.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Comparison of diazo-coupling, formazan, and silver staining techniques for visualizing alkaline phosphatase isoenzymes after electrophoresis in homogeneous-pore and gradient-pore polyacrylamide gels. 245 94

An unresolved controversy is whether exposure to organic solvents in the workplace causes hepatotoxicity. From a medical surveillance study of 289 printing factory employees who were exposed primarily to toluene, we identified eight workers who had persistently abnormal serum transaminase and/or alkaline phosphatase values. The eight men were generally healthy and gave no history of taking medications or of drinking ethanol to excess. None was obese or diabetic. Six patients had hepatomegaly based on physical examination. All eight had mild elevations (less than 2 to 3 times the upper value of normal) of serum transaminases [alanine (ALT) and aspartate aminotransferase (AST)]. However, there was a marked increase in the ratio of ALT/AST (mean = 1.61). In each case, liver biopsy revealed mild, pericentral fatty change. Our results, consistent with those previously published by some others, suggest that pericentral fatty liver with mild "reactive hepatitis" is the most likely diagnosis in workers exposed to solvents for whom common causes of mild liver test abnormalities have been excluded. An increased ALT/AST ratio may represent a convenient, previously unrecognized indicator of this condition.
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PMID:Liver structure and function in print workers exposed to toluene. 261 34

A novel enzyme-linked immunoassay employing a partitioning chromophore was developed. The assay system consisted of an aqueous phase and an immiscible organic solvent. Antigen-antibody interaction was indicated by transfer of a chromogenic indicator from the aqueous phase to an organic layer. The indicator employed was a water-soluble phosphate ester of phenylazophenol. Hydrolysis of the ester by acid or alkaline phosphatase produced a water-insoluble phenol that partitioned into toluene. The enzyme employed in this assay format can be covalently linked to antibody or a specific antibody for the phosphatase can be used. Phase change immunoassays were developed for the measurement of alkaline phosphatase, human IgG in whole blood, and the human tumor marker prostatic acid phosphatase. Solid supports of small polystyrene latex particles and Sephadex were employed.
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PMID:Phase change enzyme immunoassay. 330 Apr 12

Female Wistar rats were exposed to various solvent vapors 8 h/d for 7 d. The leukocyte suspension and serum were prepared from peripheral blood and utilized for the determination of alkaline phosphatase (AP) activity with disodium phenyl phosphate as a substrate [leukocyte AP (LAP) and serum AP (SAP) assay]. While the exposure to benzene at 20 or 50 ppm did not cause significant changes in LAP activity, the exposure at 100 and 300 ppm resulted in a dose-dependent increase of LAP activity up to more than 100% over the control. No further increase was observed at 1000 or 3000 ppm. Similar exposure at 300 ppm to either toluene, m-xylene, n-hexane, trichloroethylene, methyl ethyl ketone, ethyl acetate, or methyl alcohol did not induce any changes in LAP activity. Thus, the increase in LAP activity was considered to be specific to benzene exposure. When the animals were exposed to toluene (300 ppm) in combination with benzene (300 ppm), not only was the benzene-induced leukopenia alleviated as previously reported, but the benzene-induced increase in LAP activity was no longer observed. The parallel inhibitory effects of toluene on benzene-induced increase in LAP and leukopenia suggest that a relation may exist between increase in LAP activity and leukopenia. No changes in SAP activities were observed in the rats under the exposure conditions examined.
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PMID:Benzene-specific increase in leukocyte alkaline phosphatase activity in rats exposed to vapors of various organic solvents. 378 73

The various layers of the cell envelope of marine pseudomonad B-16 (ATCC 19855) have been separated from the cells and assayed directly for alkaline phosphatase activity under conditions established previously to be optimum for maintenance of the activity of the enzyme. Under conditions known to lead to the release of the contents of the periplasmic space from the cells, over 90% of the alkaline phosphatase was released into the medium. Neither the loosely bound outer layer nor the outer double-track layer (cell wall membrane) showed significant activity. A small amount of the alkaline phosphatase activity of the cells remained associated with the mureinoplasts when the outer layers of the cell wall were removed. Upon treatment of the mureinoplasts with lysozyme, some alkaline phosphatase was released into the medium and some remained with the protoplasts formed. Cells washed and suspended in 0.5 M NaCl were lysed by treatment with 2% toluene, and 95% of the alkaline phosphatase in the cells was released into the medium. Cells washed and suspended in complete salts solution (0.3 M NaCl, 0.05 M MgSO(4), and 0.01 M KCl) or 0.05 M MgSO(4) appeared intact after treatment with toluene but lost 50 and 10%, respectively, of their alkaline phosphatase. The results suggest that the presence of Mg(2+) in the cell wall is necessary to prevent disruption of the cells by toluene and may also be required to prevent the release of alkaline phosphatase by toluene when disruption of the cells by toluene does not take place.
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PMID:Biochemical localization of alkaline phosphatase in the cell wall of a marine pseudomonad. 481 47

Serum enzymes (aspartate transaminase, alanine transaminase, alkaline phosphatase (ALP), gamma-glutamyltransferase, and creatine kinase (CK] were measured in 296 young persons who admitted to recent inhalation of solvents, usually toluene based glues. In general, results fell within expected adult reference ranges except for ALP and CK. About 60% of subjects had CK activities above the upper reference limit and these activities were investigated in terms of their isoenzyme composition. CK B subunit activity was measured in 90 subjects with raised total CK activities. In five instances the CK B subunit activity was judged abnormal and in two subjects the presence of CK BB was confirmed. These two subjects were thought to have a circulating macro CK, type 1. It is concluded that the increased total CK activity found in this group of solvent abusers was due to physical activity, but a contribution from specific muscle toxicity by solvents cannot be excluded.
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PMID:Observed activities of serum creatine kinase: total and B subunit activity and other enzymes in young persons abusing solvents. 614 4

Reaction of N-hydroxy-2-aminofluorene (N-OH-AF) with rRNA at pH 5.0 decreased the molecular weight of the polynucleotide. Toluene-soluble aryl derivatives were released on hydrolysis of fluorenylamine- and biphenylamine-substituted RNA by treatment with venom phosphodiesterase and alkaline phosphatase. These data suggested that arylhydroxylamines, activated by incubation at pH 5.0 or by enzymatic O-acetylation, might react with the phosphate group of RNA to give unstable phosphate triesters. Spontaneous hydrolysis of these triesters would result in cleavage of the polynucleotide chain. Further enzymatic hydrolysis of the phosphate esters would yield nonpolar arylamine derivatives. Enzymatically degraded 4-aminobiphenyl(ABP)-RNA adducts were examined by high performance liquid chromatography (HPLC) for the presence of a putative phosphorylated adduct. Synthetic standards of the C-8-guanosine monophosphate-ABP adduct (ABP-GMP) and o-aminobiphenyl-O-phosphate were used as markers in the analysis of the digested RNA. A phosphate adduct of ABP was undetectable by these methods. The data also indicated that the ABP-GMP formed in the acyltransferase-mediated binding of N-hydroxy-4-acetylaminobiphenyl (N-OH-AABP) to RNA is readily degraded during the enzymatic digestion of the RNA adduct.
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PMID:Arylhydroxylamine-induced ribonucleic acid chain cleavage and chromatographic analysis of arylamine-ribonucleic acid adducts. 616 6

Conditions are described for the preparation of permeabilized cells of Candida albicans. This method has been used for the in situ assay of enzymes in both yeast cells and germ-tube forming cells. A mixture of toluene/ethanol/Triton X-100 (1:4:0.2, by vol.) at 15% (v/v) and 8% (v/v) was optimal for the in situ assay of glucose-6-phosphate dehydrogenase in yeast and germ-tube forming cells, respectively. The concentration of toluene/ethanol/Triton X-100 required for optimal in situ activity of other enzymes was influenced by the cellular location of the enzyme, growth phase and morphology. The membrane-bound enzymes (chitin synthase, glucan synthase, ATPase), cytosolic enzymes (glucose-6-phosphate dehydrogenase, isocitrate dehydrogenase, pyruvate kinase, phosphofructokinase, alkaline phosphatase, glucosamine-6-phosphate deaminase and N-acetylglucosamine kinase) and wall enzymes (beta-glucosidase and acid phosphatase) were measured and compared to the activity obtained in cell extracts. The pattern of enzyme induction and the properties of the allosteric enzymes phosphofructokinase and pyruvate kinase were measured in situ. Pyruvate kinase in situ was homotropic for phosphoenolpyruvate with a Hill coefficient of 1.9 and a S0.5 of 0.6 mM, whereas in cell extracts, it had a Hill coefficient of 1.9 and a S0.5 of 1.0 mM. The Km for ATP was 1.6 mM in cell extracts and 1.8 mM in permeabilized cells. In situ phosphofructokinase was homotropic for fructose 6-phosphate (S0.5 of 2.3 mM, Hill coefficient of 4.0). The kinetic properties of pyruvate kinase and phosphofructokinase measured in situ or in vitro were similar for both yeast cells and germ-tube forming cells.
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PMID:The in situ assay of Candida albicans enzymes during yeast growth and germ-tube formation. 631 58


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