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)

Cysteine-sensitive alkaline phosphatase and/or ouabain-sensitive Na+, K+ -ATPase were studied by ultrastructure cytochemistry in epithelial cells of proximal and distal kidney tubules. Alkaline phosphatase reactivity was confined to the surface of the microvillous luminal cell membrane of proximal tubule cells, whereas distal tubules and collecting ducts were unreactive. The Na+, K+- ATPase reactivity was localized evenly along the cytoplasmic side of the basolateral cell membrane of cells of proximal and distal tubules and in collecting ducts. In the proximal tubules, where the activity was strongest, the Na+, K+- ATPase deposits were also found in the 10--50 nm gap between the cell membrane and the cisternae of tubulo-cisternal endoplasmic reticulum (TER) underlying a major part of the basolateral cell membrane. The restriction of NA+, K+ -ATPase sites, which are involved in extrusion of Na+ from the cell, to a narrow cytoplasmic compartment located between the cell membrane and the cisternae of TER, is consistent with a transport role for the TER.
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PMID:Localization of Na+, K+ -ATPase to the inside of the basolateral cell membranes of epithelial cells of proximal and distal tubules in rabbit kidney. 625 59

The isolation of apical membranes from rat proximal colonic epithelial cells is described. Differential centrifugation yielded a 'crude' membrane fraction which was further purified using sucrose density centrifugation. The final membrane fraction was enriched 20-28-fold over homogenate in alkaline phosphatase and cysteine-sensitive alkaline phosphatase specific activities. Lipid-protein interactions and lipid dynamics examined in apical and basolateral membranes prepared from colonocytes demonstrated: (1) apical membrane, as assessed by steady-state fluorescence polarization studies have a low lipid fluidity; (2) colonic basolateral membranes possess a greater lipid fluidity than apical membranes; (3) compositional differences in these antipodal membranes appear to explain these differences in lipid fluidity; (4) fluorescence polarization studies using diphenylhexatriene detect a thermotropic transition at 21-23 degrees C in apical membranes and liposomes prepared from lipid extracts of these membranes; (5) alkaline phosphatase and L-cysteine-sensitive alkaline phosphatase activities appear to be functionally dependent on the physical state of the apical membrane's lipid.
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PMID:Protein-lipid interactions in antipodal plasma membranes of rat colonocytes. 632 87

The ultrastructural localization of alkaline phosphatase has been studied in Pacinian corpuscles of the cat mesentery by the method of Mayahara et al. (1967) with 3 substrates. As control studies, specimens were incubated in the medium containing L-cysteine (10 mmol) or EDTA (5 mmol). The electron opaque final reaction product was observed on plasmic membranes and in cytoplasm and pinocytotic vesicles of the inner core cells. The precipitate was present also in rough endoplasmic reticulum, multivesicular bodies, and cytoplasmic vacuoles of the inner core lamellae. The axon revealed the positive enzymatic activity in the axolemma and the scattered precipitate was found in axoplasm. The pinocytotic vesicles in the capillary endothelium entering Pacinian corpuscles contained the reaction product, too. The capsule lamellae were devoid of precipitate. Localization of alkaline phosphatase in pinocytotic vesicles of the inner core lamellae and capillary wall support the opinion that this enzyme plays the significant role in the phenomenon of the transport of molecules through inner core lamellae from capillaries to the axon in Pacinian corpuscles.
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PMID:The electron microscopic localization of alkaline phosphatase in Pacinian corpuscles of the cat. 642 Oct 66

A new affinity label for ribulose bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum, 2-(4-bromoacetamido)anilino-2-deoxypentitol 1,5-bisphosphate, has been prepared, Reductive amination of ribulose-P2 with p-phenylenediamine in the presence of sodium cyanoborohydride yielded an epimeric mixture which was resolved by chromatography on quaternary aminoethyl-Sephadex. Subsequent bromoacetylation of the isolated amino bisphosphates gave reagents A and B (ribo and arabino epimers of 2-(4-bromoacetamido) anilino-2-deoxypentitol 1,5-bisphosphate) which were competitive inhibitors of the carboxylase with Ki values of 705 and 104 microM, respectively. Reagent A exhibited no time-dependent effects on the carboxylase in either the deactivated or activated state. Incubation of the enzyme with reagent B in the presence of the essential activators CO2 and Mg2+, however, resulted in an irreversible, time-dependent loss of activity, with a Kinact of 125 microM and a minimal half-time of 7.3 min. Covalent incorporation of [14C]reagent B was directly proportional to the loss of activity, with total inactivation correlating with an incorporation of 1.1 mol of reagent/mol of subunit. Inclusion of the competitive inhibitor 2-carboxyribitol 1,5-bisphosphate protected against inactivation with a concomitant reduction in incorporation. Neither reagent affected the activity of spinach carboxylase. Fractionation of [14C]reagent B-modified enzyme on DEAE-cellulose, subsequent to carboxymethylation and tryptic digestion, revealed two major radioactive peaks of approximately equal area. Digestion of each peak with alkaline phosphatase and rechromatography on DEAE-cellulose resulted in pure peptides I and II. The peptides were identical except in the site of labeling: peptide I contained a modified cysteinyl residue while peptide II contained a modified histidyl residue. Automated Edman degradation established the sequence as (sequence in text) which is located near the NH2 terminus of the enzyme. The lack of reactivity with the spinach enzyme is explained by the deletion of the histidyl residue and the replacement of cysteine by tryptophan in the eukaryotic species. Although the nonconservation of the modified residues argues against a functional role other than maintenance of structural integrity, the extensive homology in this region among seven different species of carboxylase is compatible with the region comprising a portion of the active site.
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PMID:2-(4-Bromoacetamido)anilino-2-deoxypentitol 1,5-bisphosphate, a new affinity label for ribulose bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum. Determination of reaction parameters and characterization of an active site peptide. 642 17

The cellular enzyme-linked immunospecific assay (CELISA) uses ligands conjugated to calf intestinal alkaline phosphatase to quantitate antibody bound to antigens on the surfaces of whole cells. Since the endogenous alkaline phosphatase present in many cell types contributes unwanted background noise to the assay, ways of inhibiting endogenous cellular alkaline phosphatase were investigated. We found that the endogenous alkaline phosphatase in human peripheral blood mononuclear cells was incompletely inhibited by EDTA or L-cysteine. Levamisole, however, inhibited endogenous cellular alkaline phosphatase completely without impairing the sensitivity of the CELISA. The use of levamisole is recommended for assays that use alkaline phosphatase conjugates to detect molecules on the surfaces of cells that also contain endogenous alkaline phosphatase.
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PMID:Cellular enzyme-linked immunospecific assay (CELISA). IV. Inhibition of endogenous cellular alkaline phosphatase activity. 642 29

Spectrophotometric and isoelectric focusing (IEF) electrophoretic characterization of the alkaline phosphatase (ALKP) of the mosquito, Culex tarsalis, are presented. With p-nitrophenylphosphate (Pnp) as substrate, ALKP was optimally active at 37 degrees C, pH 8.0, 30 mM MgCl2, Vmax was 35.8 mumoles/10 min and the Km was 5.7 mM, with no demonstrable requirement for Zn2+. The spectrophotometric enzyme(s) was stimulated by dithiothreitol, 2-mercaptoethanol, and poly-vinylpyrollidone (PVP); inhibited by NaF, several alternative cations (Ca2+, Ba2+, Fe2+, Cu2+), and EDTA. ALKP activity was cyclic during the 15 day post-adult emergence period of the study. No significant differences were noted between the specific activities of males and females. IEF electrophoresis revealed 6 ALKP isozymes detected with alpha-naphthylphosphate within the pH range 4.0-5.5, with a second group of 3 rather indistinct species in the pH 6.0-7.0 range. IEF ALKP isozymes were stimulated by Mg2+ and PVP and inhibited by EDTA (except ALKP5.0) and cysteine; partial inhibition with phenylalanine. IEF detection of ALKP activity with Pnp indicated that the majority of the activity was localized in the pH 4.0-5.5 range, in close agreement with the alpha-naphthylphosphate results.
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PMID:Alkaline phosphatases of the mosquito, Culex tarsalis Coquillett. 646 96

Campylobacter jejuni/coli strains were isolated from the faeces of 240 patients suffering from acute enteritis. The following characteristics were investigated: (i) growth at different temperatures, and on different substrates under either microaerophilic conditions or anaerobically, with fumarate or nitrate as terminal electron acceptors; (ii) production of H2S in cysteine-containing broth; (iii) hydrolysis of hippuric acid; (iv) DNase; (v) alkaline phosphatase; (vi) beta-lactamase; (vii) presence of menaquinone; and (viii) reduction of selenite. Based on characteristics (ii)-(v), the strains could be divided in 9 phenotypical groups. Most of the strains represented group 2 (DNase+, H2S+, hippurate hydrolysis+, alk. phosphatase-) (32%), and groups 8 (DNase-, H2S+, hippurate hydrolysis+, alk. phosphatase-) (32%). The other groups were of minor importance. On the other hand, most of the isolates from the United States (Weaver, 1981) fitted well into group 1 (DNase+, H2S+, hippurate hydrolysis+, alk. phosphatase+) which might demonstrate geographical variations among C. jejuni/coli.
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PMID:Characterization of Campylobacter jejuni/coli-isolates from human faeces. 652 53

Male New Zealand White rabbits were orally given 0.05 mg of aflatoxin B1 (AFB1)/kg of body weight daily for 10 days and were treated with glutathione-precursors and depletor, antibacterial agents, or sodium thiosulfate. The drug administered, the mortality, and the mean survival time were as follows: corn-oil controls (0), euthanatized at 25 days; AFB1-controls (2), 21 days; AFB1 and saline controls (2), 22 days; cysteine and AFB1 (5), 13 days; methionine and AFB1 (5), 12 days; sodium thiosulfate and AFB1 (2), 21 days; sulfadimethoxine and AFB1 (1), 24 days; oxytetracycline and AFB1 (0), euthanatized at 25 days; and ethyl maleate and AFB1 (3), 21 days. Clinical signs of toxicosis included decreased feed consumption during AFB1 administration, loss of body weight or failure to gain, and death. Clinicopathologic changes included increases in serum bilirubin concentration and alanine aminotransferase and aspartate aminotransferase activities. Prothrombin and activated partial thromboplastin times were lengthened. Plasma fibrinogen concentration was decreased. Changes in PCV, hemoglobin concentration, and serum alkaline phosphatase were unremarkable. Oxytetracycline had protective effects against chronic aflatoxicosis in rabbits. Cysteine and methionine enhanced chronic aflatoxicosis.
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PMID:Effects of various treatments on induced chronic aflatoxicosis in rabbits. 680 40

We describe a new species of Legionella represented by 10 strains isolated from industrial cooling towers. Legionella oakridgensis differed genetically from the other seven species of Legionella in DNA hybridization studies and differed serologically in direct fluorescent-antibody tests. The new species, unlike all other species except L. jordanis, did not require added L-cysteine for growth in serial transfer on charcoal-yeast extract agar. L. oakridgensis, as well as three other species tested, required L-cysteine for primary isolation from animal tissues. L. oakridgensis was the only species of Legionella that failed to produce alkaline phosphatase at pH 8.5. In all other respects, it resembled other species of Legionella, including having a high content of branched-chain cellular fatty acids and being pathogenic for guinea pigs. These bacteria have not yet been associated with human disease, but they are potential causes of legionellosis.
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PMID:Legionella oakridgensis: unusual new species isolated from cooling tower water. 683 Feb 17

Antidotal effects of the 2 antioxidants butylated hydroxyanisole (BHA) and ethoxyquin (EQ) were evaluated in bitterweed (Hymenoxys odorata DC) toxicosis in sheep. Bitteerweed contains a toxic sesquiterpene lactone, hymenoxon, the toxicity of which is reduced by cysteine. Both BHA and EQ are known to induce hepatic glutathione production in rodents. Treatment of sheep with EQ (2.5 g/sheep/day for 9 days before poisoning) gave significant protection from toxic doses of bitterweed, but the protective effect of BHA was insignificant. Of 6 sheep given EQ in the feed, 5 survived 7 doses of bitterweed (4 g/kg/day or higher for 7 days), whereas 5 of 7 controls and 4 of 7 sheep given feed with added BHA died. The added EQ in the feed decreased the serum alkaline phosphatase activity and total protein, albumin, and calcium concentrations. Seemingly, EQ is the first protective agent with field application potential for bitterweed toxicity.
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PMID:Protective effects of antioxidants on bitterweed (Hymenoxys odorata DC) toxicity in sheep. 689 Nov 91


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