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)

Eighteen-week-old mallard hens received 0, 10, 30, 90, or 270 ppm technical grade EPN (phenylphosphonothioic acid O-ethyl-O-4-nitrophenyl ester) in the diet for 90 days. Ataxia was first observed in the 270-ppm group after 16 days, in the 90-ppm group after 20 days, in the 30-ppm group after 38 days; 10 ppm failed to produce ataxia. By the end of 90 days all 6 birds in the 270-ppm group exhibited ataxia or paralysis whereas 5 of 6 birds in the 90-ppm group and 2 of 6 birds in the 30-ppm group were visibly affected. Treatment with 30 ppm or more resulted in a significant reduction in body weight. Brain neurotoxic esterase activity was inhibited by averages of 16, 69, 73, and 74% in the 10-, 30-, 90-, and 270-ppm groups, respectively. Brain acetylcholinesterase, plasma cholinesterase, and plasma alkaline phosphatase were significantly inhibited as well. Distinct histopathological effects were seen in the 30-, 90-, and 270-ppm groups which included demyelination and degeneration of axons of the spinal cord. Additional ducks were exposed in a similar manner to 60-, 270-, or 540-ppm leptophos (phosphonothioic acid O-4-bromo-2,5-dichlorophenyl-O-methylphenyl ester) which resulted in similar behavioral, biochemical, and histopathological alterations. These findings indicate that adult mallards are probably somewhat less sensitive than chickens to subchronic dietary exposure to organophosphorus insecticides that induce delayed neurotoxicity.
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PMID:Subchronic organophosphorus ester-induced delayed neurotoxicity in mallards. 620 72

The foliate papillae of the rabbit, rat and mouse were studied by scanning electron microscopy and histochemistry. The papillae consisted of folds and grooves located on the posterolateral margin of the tongue in front of the circumvallate papillae. The numbers of folds and taste buds varied among the three animals species. Scanning electron microscopy showed that in longitudinal sections the taste buds were oval in shape and their pores were surrounded by microvilli. The reaction product of alkaline phosphatase could only be demonstrated in the superficial epithelium of the rabbit as well as in the mouse foliate papillae, but it also diffused into the taste buds in the rat. The intensity and distribution of the reactions of adenosine triphosphatase, acetylcholinesterase and butyrylcholinesterase were identical to those reported by other investigators in spite of differences in animal species and histochemical techniques employed.
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PMID:Scanning electron microscopic and histochemical studies of foliate papillae in the rabbit, rat and mouse. 621 38

The cytochemical localisation of five hydrolytic enzymes has been studied in the brain capillaries of laboratory animals. Acid phosphatase is present in primary lysosomes of endothelial cells; alkaline phosphatase activity is seen mainly on the plasma membrane of the luminal side but also in the basal lamina. The latter is also active concerning 5'nucleotidase. Butyrylcholinesterase is an enzyme synthesized by most brain capillary endothelial cells, as can be seen by intensive staining of endoplasmic reticulum cisternae. In contrast acetylcholinesterase activity at the capillaries presumably is of neuronal origin. Local neurons appear to secrete this enzyme, which then reaches the endothelial basal lamina via the extracellular spaces. From these cytochemical observations it is concluded that pinocytotic traffic in brain endothelial cells is predominantly from the brain tissue side to the luminal side.
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PMID:Enzyme cytochemistry of the cerebral microvessel wall. 630 81

After twenty weeks of continuous dosing with Trichostrongylus colubriformis larvae substantial, but declining, numbers of worms had persisted in most of the lambs examined, although there were wide inter-individual variations. Mucosal lesions were found in the proximal small intestines of all the infected animals, their severity being directly related to worm burden. Representative brush border enzyme activities analysed in intestinal mucosal extracts from the same lambs showed differing responses. Alkaline phosphatase and glycyl-L-leucine dipeptidase were significantly depleted, whereas maltase activity was only marginally reduced, and leucine aminopeptidase activity was normal. Mucosal acetylcholinesterase activity was significantly elevated in the parasitised animals and, interestingly in view of the postulated role of this enzyme in nematode pathogenicity, the level of activity was directly correlated with individual worm burdens. Intestinal trypsin and chymotrypsin activities were unaffected and the level of superoxide dismutase, an enzyme associated with the inflammatory response, was normal. There were also no consistent changes in the mucosal activities of several enzymes including lactic dehydrogenase, creatine phosphokinase, aldolase, and glutamic oxaloacetate transaminase, whose leakage from damaged or necrotic tissues has been well defined in terms of the concomitant increase in their activity in the circulation. Lambs treated orally with fenbendazole five and/or ten weeks before slaughter either in the presence or absence of continued larval intake, had negligible worm burdens, and showed little evidence of intestinal damage at post mortem. Brush border enzyme levels, with the exception of alkaline phosphatase and, in two cases dipeptidase, were normal in these animals. The activity of alkaline phosphatase was approximately double that in the continuously infected, untreated lambs, but remained markedly lower than in the uninfected controls. The activities of the other enzymes studied, including acetylcholinesterase, were within the control range. In summary, in chronic trichostrongylosis even relatively low nematode burdens were associated with marked pathological and biochemical damage in the intestine with both lesion severity and mucosal acetylcholinesterase activity being directly related to worm numbers. Although morphological integrity was completely restored after anthelmintic treatment, the persistent low activity of brush border alkaline phosphatase coupled with the enzymological findings in untreated, infected animals suggests that recovery of the full functional capability of the intestinal mucosa may take longer.
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PMID:Intestinal enzyme activity in lambs chronically infected with Trichostrongylus colubriformis: effect of anthelmintic treatment. 634 11

The synthesis of N-[5-(hydroxyethyl)dithio-2-nitrobenzoylaminoethyl] acrylamide (I) is described. If the disulfide bond in this compound is reduced with thiol reagents, an intense yellow color develops (epsilon 412 V 13,600 at pH 7.4) due to essentially the same chromophore as 5-thio-2-nitrobenzoic acid, the reduced form of 5,5'-dithiobis(2-nitrobenzoic acid)(Ellman's reagent). Polyacrylamide gels were prepared that were crosslinked with N,N'-methylenebisacrylamide and which contained I as an integral part of the polymerized acrylamide chain. Acetylcholinesterase (from electric eel and human brain tissue slices) and alkaline phosphatase (from Escherichia coli and calf intestine) were subjected to electrophoresis and then the gels were immersed in an appropriate thiol-substrate buffer (acetylthiocholine and cysteamine-S-phosphate, respectively). A yellow band developed rapidly in the acrylamide gel at the site of enzyme activity. Electrophoresis on the mixed disulfide-polyacrylamide gel proved to be a rapid and sensitive technique to detect very small amounts of enzyme (approximately 0.02 fmol acetylcholinesterase) and should have wide application for detecting other enzymes that hydrolyze thiol substrates.
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PMID:Polyacrylamide gels which contain a novel mixed disulfide compound can be used to detect enzymes that catalyze thiol-producing reactions. 636 79

The stability of various marmoset (Callithrix jacchus) plasma constituents was investigated after storage at room temperature, 4 degrees C, and -20 degrees C. The method of sequential analysis ensured that the between-run bias of the methods of analysis used was drastically reduced, and the definitions of stability were linked to the imprecision of these methods. Optimal conditions for storage for as long as 48 h depended on the analyte being measured. Room temperature was optimal for cholinesterase and acetylcholinesterase; 4 degrees C for protein, albumin, alanine aminotransferase, isocitrate dehydrogenase, sorbitol dehydrogenase, lactate dehydrogenase, and glutamate dehydrogenase; and -20 degrees C for glutathione reductase and alkaline phosphatase. For aspartate amino-transferase and gamma-glutamyltransferase, either 4 degrees C or -20 degrees C would be suitable. Reasons are advanced for some conflicting reports in the published work, and we emphasize the need to investigate each analyte and species separately.
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PMID:Stabilities of some constituents of marmoset (Callithrix jacchus) plasma under various conditions of storage. 641 8

Injectable progestogen, norethisterone enanthate (NET-EN, 200 mg/ml at 60 day intervals), was administered to 150 women for 2 years as their method of contraception. Blood levels of acid phosphatase, alkaline phosphatase, glutamate pyruvate transaminase, glutamate oxaloacetate transaminase, acetylcholinesterase (AChe), sialic acid were determined in all subjects to ascertain whether NET-EN therapy causes any adverse metabolic effect or damage to the functional status of the liver. NET-EN contraception did not alter the liver function enzymes but there is a significant increase (P0.001) in AChE activity after 2 years. Serum sialic acid level showed a transient increase up to 1 year, which however returned to control level later. The mechanism responsible for these changes and whether the rise in sialic acid and AChE activity are related to any pathological condition remain unclear at this stage.
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PMID:Studies on some enzymes and sialic acid during progestational contraceptive therapy. 646 44

The effect of malathion, an organophosphorus insecticide on tissue levels of acetylcholinesterase (Ache), phosphomonoesterases and transaminases have been studied in presence of different levels of dietary proteins. Adult male albino rats weighing 150-200 gms were given 5%, 10% and 20% protein diets containing 400 mg malathion (dust) 5% conc./kg feed for 30 days. Its effect was evaluated in liver, kidney, brain, lungs and spleen and results were compared with their respective malathion dust, pair-fed animals (5%, 10% and 20% protein groups without malathion). Animals kept on low protein diets (5% and 10%) when exposed to malathion dust showed significant increase in the activities of GOT and alkaline phosphatase in liver, kidney, brain, lungs and spleen, while a marked inhibition in the activity of Ache was observed under similar treatment. GPT was decreased in kidney and lungs, in the low protein groups (5% and 10%, whereas its activity was increased in liver, brain and spleen of animals receiving 5% protein, when exposed to compared to their respective pair-fed animals. Thus, although the degree of alteration in the enzyme profile is less severe, these changes show that high protein diet has a protective role against pesticide hazards, whereas low protein diet provides less stability to the structural integrity of the tissues.
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PMID:The effect of malathion dust on certain tissues of male rats fed varying levels of dietary protein. 649 Jan 28

Separation of the external membranes from freshly converted mechanical schistosomula of Schistosoma mansoni was achieved by osmotic shock under hypertonic conditions, followed by mechanical shearing and ultracentrifugation. Prior to treatment, the schistosomula were surface labeled by introduction of N-DNP-epsilon-aminocaproylphosphatidylethanolamine molecules into their lipid bilayer followed by anti-DNP antibodies and stained with either 125I-protein-A or ferritin labeled secondary anti-DNP antibodies. This label provided a membrane marker by which the purity of the preparation could be assessed at each stage. Fluorescence staining with FITC-conjugated secondary antibodies prior to treatment revealed that the homogeneously stained membrane of the intact schistosomula became swollen and ruptured after the osmotic shock. The isolated membrane pellet was intensely fluorescent. Electron microscopical examination revealed mostly vesicles, some of them with organized multilayer assembly. The vesicles were ferritin labeled, indicating that they originated from the outer surface membrane of the schistosomula. A 100 fold enrichment in the alkaline phosphatase activity and about 300 fold enrichment in acetylcholinesterase activity in the membrane preparations, as compared to the intact schistosomula, was found. The isolated tegument was analyzed by SDS-polyacrylamide gel electrophoresis. The pattern obtained showed three major bands, of molecular weights 69 000, 45 000 and 12 000 alongside with a large number of minor bands. Immunoprecipitation of the isolated 125I-labeled membrane antigens with antisera from chronically infected mice revealed these three major bands together with three other bands of molecular weight 38 000, 23 000 and 16 000.
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PMID:Isolation and partial characterization of the tegumental outer membrane of schistosomula of Schistosoma mansoni. 652 92

A series of affinity chromatography packings for the purification of serine and sulfhydryl esterases (acetylcholinesterase, alkaline phosphatase, urokinase and papain) have been synthesized using commercially available agarose, glass and acrylate parent matrices. Two ligands were coupled to the matrices by utilizing carbodiimide or reaction with active groups already present on the matrix: the quaternary ammonium compound trimethyl(p-aminophenyl)ammonium chloride and the serine esterase inhibitor analog p-aminobenzamidine. It was found that enzyme purification on the agarose- or acrylate-based packings was most successful, resulting in as much as fifty-fold purification over starting material. The pressure stability of the acrylate packing allowed purification by high-pressure affinity chromatography and decreased purification times as much as six-fold in comparison to agarose columns.
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PMID:Comparison of low- and high-pressure affinity chromatography for the purification of serine and sulfhydryl esterases. 653 Apr 33


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