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)

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 proposed system of continuous monitoring of enzyme activities is based primarily on the electrochemical behaviour of thiol compounds, and the experimental equipment is extremely simple. The determination of cholinesterase (EC 3.1.1.8) activity is described. The normal values obtained for men (73.9, s +/- 10.3 microkat/l) and for women (71.1, s +/- 10.2 microkat/l), lie within the usual range of analogous photometric methods. Systems for determination of the activities of alkaline phosphatase (EC 3.1.3.1) and adenosylhomocysteinase (EC 3.3.1.1) are described. The activity of aspartate aminotransferase (EC 2.6.1.1) is determined by a combination of enzyme reactions, in which CoA is released from acetyl-CoA. Analogous procedures are discussed for determinations of alanine aminotransferase (EC 2.6.1.2), lactate dehydrogenase (EC 1.1.1.27), lipase (EC 3.1.1.2), and phospholipase A2 (EC 3.1.1.4) activities, and for determination of substrates, e.g., acetate and carnitine. Possible determinations of an additional 199 enzyme activities and of some of substrates are suggested. By determining electrochemically active groups other than thiols this method becomes almost universally applicable.
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PMID:New system of continuous monitoring of enzyme activities and determination of some substrates. 344 Aug 58

Venoms from 20 species of stinging Hymenoptera, including nine species of ants and nine species of social wasps, were quantitatively analyzed for the following enzymic activities: phospholipase A, hyaluronidase, lipase, esterase, protease, acid phosphatase, alkaline phosphatase and phosphodiesterase. Phospholipase and hyaluronidase were present in all the venoms, with activity levels generally higher among the wasps than the ants (P less than 0.05). Lipase was present in high activity in several social wasp venoms and one ant venom, in low levels in two other ant venoms and absent from four tested snake venoms. Two-carbon esterase activity was present in the venoms of five social wasps and one ant. Non-specific protease was present at very high activity levels in the venoms of an army ant species and was also present in the venoms of a social wasp and another ant. Acid phosphatase activity was present in eight of the nine ant venoms, but was essentially absent from all the social wasp venoms. Alkaline phosphatase activity was clearly detectable in the venoms of only two species of ants. Phosphodiesterase, an enzyme not previously detected in insect venoms, was present in the venoms of three closely related ant species. Venoms with generally high enzymic activities included those of Polistes infuscatus, Vespula (V.) squamosa and Pogonomyrmex badius; those with low activities included Dolichovespula maculata, Apoica pallens and Dasymutilla lepeletierii. The 20 venoms were ranked according to overall activity levels using the eight enzyme activities plus lethal, hemolytic and pain-inducing activities. They were also compared phylogenetically using these 11 activities.
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PMID:Comparative enzymology of venoms from stinging Hymenoptera. 354 39

The anti-inflammatory activity of Cassia occidentalis leaf powder and an ethanol extract of Cardiospermum halicacabum aerial parts were assayed in male albino rats using carrageenan-induced rat paw edema. C. occidentalis was maximally active at a dose of 2000 mg/kg, while the C. halicacabum extract was maximally effective at a dose of 500 mg/kg. In the cotton pellet granuloma assay, these drugs were able to suppress the transudative, exudative and proliferative components of chronic inflammation. Further, these drugs were able to lower the lipid peroxide content and gamma-glutamyl transpeptidase and phospholipase A2 activity in the exudate of cotton pellet granuloma. The increased alkaline phosphatase activity and decreased A/G ratio of plasma in cotton pellet granulomatous rats were normalized after treatment with these drugs. C. occidentalis powder and C. halicacabum extract were able to stabilize the human erythrocyte membrane against hypotonicity-induced lysis. It is likely that these drugs may exert their anti-inflammatory activity by inhibition of phospholipase A2, resulting in the reduced availability of arachidonic acid, a precursor of prostaglandin biosynthesis, and/or by stabilization of the lysosomal membrane system.
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PMID:Biochemical modes of action of Cassia occidentalis and Cardiospermum halicacabum in inflammation. 361 9

The enzyme contents of four venom samples of Calloselasma rhodostoma were analyzed. The venoms contained phosphodiesterase, alkaline phosphomonoesterase, 5'-nucleotidase, protease, phospholipase A, L-amino acid oxidase, hyaluronidase, arginine ester hydrolase, arginine amidase, fibrinogenase and coagulant enzyme activities. There is significant variation in the contents of coagulant enzyme, arginine ester hydrolase, hyaluronidase, protease, phosphodiesterase, alkaline phosphomonoesterase and L-amino acid oxidase. DEAE-Sephacel ion exchange chromatography of the venom resolved it into eight major protein fractions. The eight fractions were heterogeneous and exhibited more than one type of enzymatic activity. The 5'-nucleotidase, alkaline phosphomonoesterase, protease, coagulant enzyme, arginine ester hydrolase, arginine amidase and fibrinogenase exist in multiple forms.
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PMID:Enzymatic activities of Calloselasma rhodostoma (Malayan pit viper) venom. 375 Mar 51

1. Lysolecithin, prepared by the action of snake-venom phospholipase A on ovolecithin, when incubated with Savoy-cabbage phospholipase D, in the presence of Ca(2+) ions, gave two degradation products (designated A and B) in the form of their calcium salts. 2. These calcium salts were separated quantitatively by solvent fractionation and converted into the corresponding sodium salts. 3. Substance B proved to be a lysophosphatidic acid of conventional structure (1-monoacyl-l-3-glycerophosphoric acid). When the phosphate group was removed by means of prostatic acid phosphomonoesterase, a 1-monoglyceride was formed quantitatively. Alkaline hydrolysis gave the theoretical yield of l-3-glycerophosphate. 4. Substance A, on the other hand, had all the properties expected for a cyclic phosphate of a 1-monoglyceride. It was unaffected by phosphomonoesterase. On alkaline hydrolysis, the acyl group was removed and ring opening of the presumed cyclic phosphate group gave an approximately equimolar mixture of 2- and l-3-glycerophosphates. 5. The structures of substances A and B confirm lysolecithin as 1-monoacyl-l-3-glycerylphosphorylcholine.
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PMID:The chemical nature of the products obtained by the action of cabbage-leaf phospholipase D on lysolecithin: the structure of lysolecithin. 429 59

The cytoplasmic membrane of Mycoplasma laidlawii strain B is solubilized by anionic and nonionic detergents, succinylation, phospholipase A, alkaline phosphatase, trypsin, and chymotrypsin. Cationic detergents are without effect, as are chelating agents, even in the presence of high concentrations of monovalent cation. The detergent-solubilized membrane exhibits one peak in the analytical ultracentrifuge, but the sedimentation coefficient is dependent upon concentration of detergent. Simple dialysis does not remove all of the sodium dodecylsulfate except from lipid-depleted membrane particles. Membranes bind sodium dodecylsulfate but acetone powders of membranes do not. Sulfated alcohols with chain lengths of C(14) and C(16) are more tightly bound than dodecylsulfate. A constant amount of di- and trivalent cation is bound by the membrane upon aggregation. Only a portion of this cation is removable with chelating agents. No chelating agent is bound by these aggregates. A portion of the lipid-depleted membrane particles is solubilized by negatively charged lipids and detergents, giving rise to aggregates in the presence of divalent cation. Fractionations of detergent-solubilized membranes by preparative gel electrophoresis and ammonium sulfate were inconclusive. Density gradient centrifugation of succinylated membranes yielded at least five fractions which exhibited homogeneity by ultracentrifugation. Analytical gel electrophoresis of these fractions demonstrated heterogeneity. The composition of these five fractions suggested separation of protein from lipid.
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PMID:Observations on membranes of Mycoplasma laidlawii strain B. 536 Dec 9

The influence of two surface-active food additives on the integrity and permeability of rat ileal mucosa has been studied. We determined the activity of N-acetyl-beta-glucosaminidase, a lysosomal enzyme, in the rat intestinal lumen after deposition of polyoxyethylene (20) sorbitan monostearate (polysorbate 60; Tween 60) or polyoxyethylene (20) sorbitan monooleate (polysorbate 80; Tween 80) in a section of ligated, cannulated gut. We also determined the activities of N-acetyl-beta-glucosaminidase, alkaline phosphatase, 5'-nucleotidase and phospholipase A2 in mixtures of isolated mucosal cells and polysorbate 60 or polysorbate 80. The activity of N-acetyl-beta-glucosaminidase was increased in the luminal contents of the cannulated gut 15 min after deposition of either polysorbate 60 or polysorbate 80 (10 mg/ml fluid instilled into gut). It was also increased in mixtures of mucosal cells and polysorbate 60 or polysorbate 80 (0.1-10 mg/ml). In contrast, the activities of alkaline phosphatase and 5'-nucleotidase were unaffected and that of phospholipase A2 was decreased by the presence of either polysorbate. These findings indicated that polysorbate 60 and polysorbate 80 released lysosomal enzymes from the intestinal mucosal cells and that these agents might damage the intestinal mucosa and increase its permeability. We therefore determined the intestinal permeability to sodium fluorescein in the absence and presence of polysorbate 60 or 80 and found that the permeability was slightly increased in the presence of either of the compounds at concentrations of 10 mg/ml fluid instilled into gut. It is possible therefore that surface-active food additives might impair the function of the mucosal barrier and increase the permeability of the gut to potentially toxic and pathogenic molecules.
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PMID:Influence of surface-active food additives on the integrity and permeability of rat intestinal mucosa. 609 20

1,2-Diacyl-sn-glycerol : CDPcholine cholinephosphotransferase (EC 2.7.8.2) and acyl-CoA : 1-acyl-sn-glycero-3-phosphocholine acyltransferase (EC 2.3.1.23) activities of rat liver microsomes can be inhibited by centrophenoxine (N,N-dimethylaminoethyl p-chlorophenoxyacetate). This inhibition is brought about by the intact centrophenoxine molecule rather than by the products of hydrolysis. A nonhydrolyzable ether analog of centrophenoxine was synthesized (neophenoxine; N,N-dimethylaminoethyl p-chlorophenoxyethyl ether) and proved most effective in inhibiting the two routes of phosphatidylcholine biosynthesis. While 50% inhibition of the cholinephosphotransferase was attained at 5 mM neophenoxine, 50% inhibition of the acyltransferase required 0.6 mM neophenoxine levels only. Inhibition of the cholinephosphotransferase (Ki approximately 1.5 mM) and the acyltransferase (Ki approximately 1 mM) by neophenoxine was shown to be noncompetitive. Other membrane-bound enzymes, such as glucose-6-phosphatase, monoacylglycerol lipase, alkaline phosphatase or phospholipase A2 were not affected by the inhibitors. Because of this specificity, and because of the high affinity of the microsomal membrane for such agents, centrophenoxine and neophenoxine should prove useful for controlling phosphatidylcholine synthesis and for modulating the phosphatidylcholine deacylation-reacylation cycle.
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PMID:Modulation of phosphatidylcholine synthesis in vitro. Inhibition of diacylglycerol cholinephosphotransferase and lysophosphatidylcholine acyltransferase by centrophenoxine and neophenoxine. 626 46

The effect of bactericidal concentrations of lysozyme-free human serum on parameters of membrane integrity has been studied in serum-susceptible and serum-resistant Escherichia coli strains. Serum treatment released all of the alkaline phosphatase from the periplasmic space of two rapidly serum-susceptible strains but did so at different rates. In contrast, no periplasmic enzyme was released from two serum-resistant strains or from one moderately susceptible smooth strain. Lysozyme-free serum and heat-inactivated serum released comparable amounts of 86Rb+ from preloaded cells at comparable rates, regardless of serum susceptibility. Serum decreased the rate of phospholipid biosynthesis in both serum-susceptible and serum-resistant strains. In susceptible but not in resistant strains, intracellular ATP pools were depleted after serum exposure. Outer membranes and cytoplasmic membranes were prepared from serum-treated E. coli, and assays for C3 and C5b-9(m) were performed. With rapidly susceptible strains, C3 deposition on the outer membrane without attachment of C5b-9(m) occurred during the short prekilling phase. Subsequent bacterial killing was accompanied by deposition of C5b-9(m), which was recovered with C3 exclusively in outer membrane fractions with increased density and by eventual total loss of recoverable cytoplasmic membranes. Minimal deposition of complement components, without accompanying cytoplasmic membrane loss, occurred with serum-resistant strains. Loss of recoverable cytoplasmic membrane was not due to the action of either serum or bacterial phospholipase A. The results raise the possibilities that C5b-9(m) primarily damages the outer membrane and that the bacteria themselves actively participate in the ensuing, as yet unclarified, metabolic reactions that finally lead to their death.
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PMID:Membrane changes induced by exposure of Escherichia coli to human serum. 635 36


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