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:3.1.3.5 (5'-nucleotidase)
3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

1. The L-amino acid oxidase, hyaluronidase, alkaline phosphomonoesterase, protease, phosphodiesterase, acetylcholinesterase, phospholipase A and 5'-nucleotidase activities of 47 samples of venoms from all the six species of cobra (Naja), including five subspecies of Naja naja, were examined. 2. The results demonstrated interspecific differences in the venom contents of phospholipase A, acetylcholinesterase, hyaluronidase and phosphodiesterase. These differences in venom enzyme contents can be used for the differentiation of species of the genus Naja. 3. Thus, our results revealed a correlation between the enzyme composition of venom and the taxonomic status of the snake at the species level for the genus Naja.
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PMID:A comparative study of cobra (Naja) venom enzymes. 285 66

A rat brain P3 fraction enriched in ER derived microsomes was centrifuged through a 20-40% linear sucrose gradient in a Beckman Ti-14 Zonal rotor and 11 fractions were obtained. The distribution of marker enzyme activities and protein were determined in these 11 subfractions. NADPH-Cytochrome C reductase, choline phosphotransferase were employed for endoplasmic reticulum, Na+,K+-ATPase, 5'-nucleotidase, and acetylcholinesterase were employed for plasma membrane, 2',3'-cyclic nucleotide phosphohydrolase was employed for myelin. The bulk of the protein was recovered in the 24-34% sucrose fractions, Na+,K+-ATPase, 5'-nucleotidase, and acetylcholinesterase were in the 22-38% sucrose fractions while NADPH-cytochrome C reductase and CNPase were enriched in the 20-22% sucrose fractions. The ethanolamine and the serine base exchange activities had a bimodal distribution, with highest specific activities in sucrose fractions 32-34% and 20-24%. Choline base exchange activity was nearly undetectable in all the fractions. The specific activities of CDP-choline phosphotransferase, and phospholipid-N-methyltransferase were highest in the 20-22% sucrose fraction. Phospholipid-N-methyltransferase activity was significantly stimulated in the presence of exogenous phospholipid acceptors as phosphatidylethanolamine or phosphatidylmonomethylethanolamine or phosphatidyldimethylethanolamine, however, the greatest response was with phosphatidylmonomethylethanolamine. The rat brain P3 fraction yielded a population of a membrane at the light end of the sucrose gradient which has a buoyant density similar to myelin but seemed to be enriched with NADPH cytochrome C reductase and phospholipid modifying enzymes. This is in contrast to liver microsomes submitted to a similar fractionation.
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PMID:Distribution of selected phospholipid modifying enzymes in rat brain microsomal subfractions prepared by density gradient zonal rotor centrifugation. 298 22

Neuronal membrane enzyme activities were determined in naive and ethanol-treated (30 min after 2 g/kg) male and female rats of lines developed for more (ANT) and less (AT) ethanol-induced motor impairment. Ethanol did not affect acetylcholinesterase, (Na+K)-ATPase or 5'-nucleotidase activities, but adenylate cyclase activities were lowered in both cerebellum and cerebrum. Cerebral acetylcholinesterase activities were higher in ANT than AT rats. No consistent line difference was observed regarding (Na+K)-ATPase activities. Slightly higher cerebellar 5'-nucleotidase activities were found in the ANT line. Cerebellar adenylate cyclase levels were substantially higher in the AT line. No line differences were displayed in the activation of adenylate cyclase activity by dopamine or norepinephrine. It is concluded that ethanol in vivo may inhibit neuronal adenylate cyclase activity and that cerebellar phosphorylation may be a regulator of motor impairment. Cholinergic mechanisms may also be connected to the ethanol-induced motor impairment.
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PMID:Neuronal membrane enzymes in rat lines selected for differential motor impairment by ethanol. 301 92

Many questions concerning the morphology of the spleen have been cleared up in the last 20 years by the application of new methods of investigation, especially electron microscopy and enzyme histochemistry. With but a few exceptions, however, only the splenic parenchyma (the red and white pulp) were studied. Such special structures of the human spleen as nerves, lymphatic vessels and their supporting tissue, which may play an important role in the coordination and integration of the different functions of the white pulp (secondary lymphatic organ) and the red pulp (blood filter), were hardly ever studied with modern techniques. Investigating these structures light and electron microscopically and enzyme histochemically it was attempted to complete our present knowledge of the histology of the human spleen. In addition, by comparing the study of special altered spleens with experimental data it was attempted to clarify the importance of these structures for the physiology and pathology of the spleen. A total of 151 normal and pathologically altered spleens from the bioptic and autopsy material of the Pathological Institute of the University of Kiel were examined. In addition to conventional light microscopy the spleens were investigated enzyme histochemically and cytochemically, fluorescence microscopically and electron microscopically. The following enzyme reactions were done: Alkaline and acid phosphatase, alpha-naphthylacetate-esterase, naphthol-AS-acetate-esterase, 5'-nucleotidase, ATPase, and acetylcholinesterase. The various enzyme reactions were sometimes done in combination and reticulum and collagenous fibers were investigated by a subsequent staining of argyrophilic fibers. The fine localization of the 5'-nucleotidase activity was studied ultrahistochemically. Adrenergic nerve fibers were investigated fluorescence microscopically using the glyoxylic acid method.
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PMID:[Morphology and function of the human spleen. Enzyme histochemical and electron microscopy studies of the splenic lymphatic vessels, nerves and connective tissue structures]. 305 73

The activities of various enzymes present in brain homogenates were assayed biochemically (a) with no pretreatment, (b) following a standard microwave treatment in saline and (c) after a standard microwave treatment in formalin. All enzyme activity was lost after the microwave - formalin in treatment. Following microwave - saline treatment, the activities of alkaline phosphatase, 5'-nucleotidase, isocitrate and succinate dehydrogenases were reduced. In contrast, the activities of lactate and malate dehydrogenases were unchanged, and that of acetylcholinesterase apparently increased. Analogous outcomes were seen following attempted histochemical demonstrations of these enzymes. Thus satisfactory histochemical demonstration of all enzymes was achieved (except with alkaline phosphatase, lactate and malate dehydrogenases) following the microwave-saline pretreatment. Since acid phosphatase, catalase and peroxidase were also successfully demonstrated, it seems that microwave-saline pretreatments permit both retention of sufficient enzyme activity for histochemical demonstration to occur and retention of sufficient structural integrity for critical morphological investigations. Since the failure to stain the sites of lactate and malate dehydrogenases is not due to microwave inactivation of these enzymes, their demonstration may be possible by varying the staining procedures.
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PMID:Brain enzyme histochemistry following stabilization by microwave irradiation. 306 7

The toxic and biological activities of four samples of Trimeresurus purpureomaculatus venom were examined. The lethality, protein composition and biological activities of the four venom samples were similar. Three of the venom samples had LD50 (i.v.) values of 0.9 micrograms/g while the fourth had a lower LD50 (i.v.) of 0.45 micrograms/g. All four venom samples exhibited hemorrhagic, edema-inducing, anticoagulant and thrombin-like activities as well as the usual enzymes found in crotalid venoms. DEAE-Sephacel ion exchange chromatographic fractionation of the venom yielded 10 protein fractions. Only two fractions (fractions A and F) were lethal to mice; the major lethal fraction being fraction F. This fraction had an LD50 (i.v.) of 0.2 micrograms/g and exhibited hemorrhagic, edema-inducing and thrombin-like activity. It also exhibited phospholipase A, arginine ester hydrolase, arginine amidase, protease, 5'-nucleotidase, acetylcholinesterase and alkaline phosphomonoesterase activities. The lethal potency of fraction F is potentiated by fraction G, which exhibited anticoagulant activity as well as hemorrhagic, edema-inducing and enzymatic activities. Fractions F plus G account for almost 100% of the lethal potency of the venom.
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PMID:Biological properties of Trimeresurus purpureomaculatus (shore pit viper) venom and its fractions. 324 58

The enzymatic activities of four samples of Malayan cobra venom were investigated. There was significant variation in the contents of L-amino acid oxidase, alkaline phosphomonoesterase, acetylcholinesterase, phospholipase A, 5'-nucleotidase and hyaluronidase. The phosphodiesterase content was, however, constant. Storage of the lyophilized venom powder at 25 degrees C for 1 month did not affect the enzymatic activities. The venom enzymatic activities were generally also stable at 4 degrees C in 0.85% saline solution. After incubation at 37 degrees C for 39 days in 0.85% saline solution, the venom still retained considerable amounts of enzymatic activities. SP-Sephadex C-25 ion-exchange chromatography of the venom showed that the phospholipase A, L-amino acid oxidase, 5'-nucleotidase, phosphodiesterase and alkaline phosphomonoesterase exist in multiple forms.
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PMID:Enzymatic activities of Malayan cobra (Naja naja sputatrix) venoms. 343 96

The rat brains homogenized with different media (sucrose, ethylene glycol, dimethyl sulfoxide and urea) yielded different amounts of microsomal fractions. The dielectric constant, density and viscosity of the homogenization media did not correlate with the amount of microsomes separated by differential centrifugation. The homogenization media containing dimethyl sulfoxide were the most efficient for the isolation of rat brain microsomes. The increase in the yield was up to 4-fold when 50% (v/v) dimethyl sulfoxide was employed. Microsomes isolated in this manner were analogous to those obtained from isotonic sucrose solution, as was demonstrated by their chemical and enzymatic (5'-nucleotidase, adenosine deaminase, guanine deaminase, purine-nucleoside phosphorylase, lactate, malate and glutamate dehydrogenases, amine oxidase fumarate hydratase, acid and alkaline phosphatase, acetylcholinesterase, NADPH-cytochrome c reductase, catalase and thiamine-diphosphatase) characterization.
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PMID:An improved method for the preparation of rat brain microsomes. 371 74

Vesiculated fragments of presynaptic plasma membranes have been isolated from the purely cholinergic electromotor nerve terminals of Torpedo marmorata. Synaptosomes, generated from the terminals by homogenization, were separated on a discontinuous Ficoll gradient and then lysed by osmotic shock at 2 degrees C, pH 8.5 in the presence of 0.1 mM MgCl2. These conditions for lysis were optimal for choline transport. Electron micrographs of lysed synaptosomes showed vesiculated membranes with diameters smaller than those of synaptosomes; occasionally, synaptic vesicles were observed attached to them. Intact mitochondria or synaptosomes and basal laminae were not present. High-affinity (KT = 1.7 microM) uptake of choline into these vesiculated membrane fragments showed: an absolute dependence on the Na+ gradient (outside greater than inside), a transient Na+-gradient-dependent accumulation of choline over the equilibrium concentration (over-shoot), electrogenicity and rheogenicity, since the uptake was further stimulated in the presence of a Na+ gradient by valinomycin, dependence on the presence of external Cl-, and partial dependence on a Cl- gradient (outside greater than inside), high-affinity (Ki = 25 nM) inhibition by hemicholinium-3 and temperature sensitivity. The plasma membranes were further purified by centrifugal density gradient fractionation on a 4-12% Ficoll gradient. Several enzymes and polypeptides copurified with the specific binding sites for choline present in the membranes. The fraction with the most binding sites was one denser than 12% Ficoll. This was also the fraction richest in acetylcholinesterase, 5'-nucleotidase and polypeptides of relative molecular mass, Mr (X 10(-3)) of greater than 200, 140, 68 (doublet), 57, 54 and 28. Acetylcholinesterase was positively identified as a Mr 68 000 component by immune blot. By contrast the ouabain-sensitive ATPase showed a negative correlation with choline binding sites. When the solubilized proteins of the vesiculated membranes were transferred to liposomes, they conferred on the latter the capacity to take up choline in a manner closely resembling its transport in natural membranes but with an initial (one minute) rate of uptake approximately 10-times greater per mg of protein. Several proteins were selectively transferred to the liposomes including ones of Mr (X 10(-3)) 34, 42, 47, 54, 60, 68, 92, 160 and greater than 200. The polypeptides of Mr (X 10(-3)) 140, 57 and 28 were lost in the transfer.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:High-affinity, sodium-gradient-dependent transport of choline into vesiculated presynaptic plasma membrane fragments from the electric organ of Torpedo marmorata and reconstitution of the solubilized transporter into liposomes. 398 97

1. Formation of phosphatidic acid by diglyceride kinase (EC 2.7.1.-) in the presence of ATP and Mg(2+) was shown in a homogenate and subcellular fractions of rat cerebral cortex. 2. The kinase was activated by Mg(2+). Ca(2+) activated to a smaller extent but was inhibitory in the presence of optimum concentration of Mg(2+). Activity was greatly increased in the presence of added 1,2-diglyceride. 3. Sodium deoxycholate markedly stimulated the reaction, but other detergents (Cutscum and Triton X-100) did not. 4. Diglyceride kinase was concentrated in the supernatant and microsomal fractions from rat cerebral cortex. The distribution of the kinase in the particulate fractions resembled that of acetylcholinesterase and 5'-nucleotidase. 5. The rate of phosphatidic acid synthesis by the diglyceride kinase route was much greater than reported rates for acylation of 3-glycerophosphate and was also very rapid in comparison with the rates of other steps in the synthesis of phosphoinositides. 6. Acetylcholine had no stimulatory effect on diglyceride kinase of isolated intact nerve-ending particles or of nerve-ending membranes obtained after osmotic shock.
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PMID:The diglyceride kinase of rat cerebral cortex. 511 67


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