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 administration of [3H]BPDE-DNA, whether by i.p. or i.v. injection, to male Wistar rats resulted in the majority of the radioactivity being recovered in the faeces. Excretion was rapid: within 24 h post-injection, 45% of the applied dose was recovered in the faeces. H.p.l.c. analysis of radioactive material extracted from the faeces by methanol showed that it contained a single component which co-chromatographed with [3H]BPDE-dGuo and which was not affected by treatment with alkaline phosphatase, aryl sulphatase or beta-glucuronidase. To determine if this phenomenon occurs after topical application of BP to a target tissue, such as mouse skin, animals were treated with [3H]BP and their faeces collected. After an extensive extraction procedure involving differential solubility in organic solvents, Sephadex LH-20 chromatography and h.p.l.c., a product was isolated from mice faeces which had characteristics consistent with a [3H]BPDE-dGuo adduct. These findings are discussed in relation to detection of BPDE adducts in human populations.
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PMID:Topical treatment of mice with benzo[a]pyrene or parenteral administration of benzo[a]pyrene diol epoxide-DNA to rats results in faecal excretion of a putative benzo[a]pyrene diol epoxide-deoxyguanosine adduct. 311 51

Immunohistochemical and histochemical methods are increasingly used and their application in surgical pathology is obvious. Especially we used these methods on bone marrow core biopsies. Optimal and comparable results have been obtained by using different methods after halving the biopsy cores longitudinally and/or transversally. The two halves were used for cytologic imprints. Two parts of the biopsy cores were embedded in polymethacrylate at low temperature (-20 degrees C). The methacrylate-embedded biopsy part for routine histology was fixed in Schaffer's solution (methanol-formalin-fixative). The methacrylate-embedded undecalcified section of 4 microns may be stained by most stains commonly employed in routine histopathology after removal of the plastic. The sections are virtually free of artefacts such as shrinkage and swelling in the light microscope. The second methacrylate-embedded part of biopsy cores was fixed in 2% paraformaldehyde with 5% sucrose in 0.02 M phosphate buffer (pH 7.4) and dehydrated in ethyleneglycolmonobutylether. All procedures were carried out at 4 degrees C. This method permits the use of immunohistochemical and histochemical procedures. The immunohistochemistry was carried out at sections of 4 microns after removal of the plastic with methoxide and use of proteolytic enzyme (0.1% alpha-chymotrypsin) to unmask antigens in sections. Surface and intracellular immunoglobulins were very well detected with the indirect FITC method. The histochemical procedures are carried out at sections of 7-8 microns after removal of plastic with xylene and toluol. The sections were incubated for specific esterase and nonspecific esterases, acid and alkaline phosphatase and then examined by light microscopy. A third part of biopsy cores may be immediately frozen, and cryostat sections are stained and evaluated for rapid diagnosis and used for immunohistologic analysis with mono- and polyclonal antibodies (FITC method) and/or histochemical investigations. Imprints of biopsy cores are evaluated for cytological, cytochemical and/or immunocytological analysis with mono- and polyclonal antibodies (FITC method). The cryostat sections and the imprints are fixed for all methods with 2% paraformaldehyde and 5% sucrose in PBS (0.02 M, pH 7.4) at 4 degrees C for 30 minutes. The best diagnostic results were obtained in the myelo- and lymphoproliferative disorders using the combination of methods described here. Examples were demonstrated.
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PMID:[Immuno- and enzymehistochemical studies of methacrylate-embedded biopsy material, especially iliac crest biopsies]. 313 12

The aim of this study was to evaluate methods of labeling the perfused cerebral capillary bed using fluorescein isothiocyanate (FITC)-dextran or FITC-globulin. An alkaline phosphatase stain was used to identify the total capillary bed. All experiments were conducted on anesthetized rats. FITC labels were injected and the rats were sacrificed either 20 sec or 6 min after injection. Heads were frozen in liquid N2 or dry ice-cooled methanol. An additional group was perfused with India ink. Comparisons were made between FITC labels and methods of slide analysis. No significant differences in cerebral capillary number per square millimeter or volume per cubic millimeter were found in animals in which the heads were frozen in liquid N2 or dry ice-cooled methanol. in FITC labels, or in light sources. When sections were air dried, 56 +/- 4% of the alkaline phosphatase stained vessels were marked with FITC label in brains frozen 20 sec after FITC injection. India ink labeled 89 +/- 7% of the alkaline phosphatase stained capillaries. When sections were air dried, 86 +/- 7% of the alkaline phosphatase stained vessels were labeled in brains frozen 6 min after injection of the FITC label. Using a technique of absolute alcohol impregnation of the sections, 130 +/- 25% and 144 +/- 28% of the alkaline phosphatase stained sections were FITC labeled. It can be concluded that the absolute alcohol impregnation technique significantly overestimates the number of perfused cerebral capillaries.
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PMID:Measurement of cerebral capillary perfusion with a fluorescent label. 314 46

We have noted two previously undescribed inositol polyphosphates in neutral methanol extracts from Swiss mouse 3T3 cells that were grown in [3H]inositol and stimulated with platelet-derived growth factor. They have been identified as 1-monomethylphosphoinositol 4,5-bisphosphate and 1-monomethylphosphoinositol 4-phosphate by comparison to a synthesized standard using HPLC chromatography, paper electrophoresis, and enzymatic dephosphorylation with inositol polyphosphate 5-phosphomonoesterase and intestinal alkaline phosphatase [orthophosphoric-monoester phosphohydrolase (alkaline optimum), EC 3.1.3.1]. We propose that these compounds are formed by methanolysis of inositol 1,2-(cyclic)-4,5-trisphosphate and inositol 1,2-(cyclic)-4-bisphosphate present in the cells. Inositol cyclic phosphates did not react with neutral methanol in the absence of the cells, which are required for the methanolysis reaction. These findings suggest a role for inositol cyclic phosphates as reactive compounds that are added to as yet unidentified cellular acceptors.
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PMID:Isolation of 1-monomethylphosphoinositol 4,5-bisphosphate [a product of methanolysis of inositol 1,2-(cyclic)-4,5-trisphosphate] from Swiss mouse 3T3 cells. 342 29

The conformations of a synthetic peptide corresponding to the signal sequence of E. coli alkaline phosphatase, Lys-Gln-Ser-Thr-Ile-Ala-Leu-Ala-Leu-Leu-Pro-Leu-Leu-Phe-Thr-Pro-Val-Thr- Lys- Ala-OCH3, have been examined in different environments by circular dichroism spectroscopy. In trifluoroethanol, methanol and aqueous mixtures of these solvents, the signal peptide has largely random conformation (approximately 80%) with small amounts of alpha-helix and beta-structure. However, in micellar environment, there is a significant increase in ordered conformation with both alpha-helix and beta-structure being present, unlike in other signal sequences reported in the literature, where only the alpha-helical conformation has been observed. Hence, an alpha-helical conformation may not be as stringent a requirement as overall hydrophobicity for recognition of signal sequences by the cell's export machinery.
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PMID:Circular dichroism studies on the signal sequence of E. coli alkaline phosphatase indicate the presence of both alpha-helix and beta-structure in hydrophobic environments. 352 76

EDTA-treated Rhizobium trifolii cells (strain NA30) incorporate radioactivity from (14C) labeled UDP-Clc, UDP-ClcA, Acetyl-Coa and/or phosphoenol pyruvate into chloroform: methanol: water (1:2:0.3) extracts. The incorporation products have properties of prenyl-phospho-sugars; mild alkaline hydrolysis of these extracts produce cyclic phosphate esters suggesting the presence of a diphosphate bridge, and mild acid or catalytic reduction-alkaline phosphatase treatments release four main components a, b, c and d, as judged by paper electrophoresis and chromatography and gel filtration studies. The four components can be obtained (14C)acetyl-labeled, but only compound c and to a lesser degree compound b can be (14C)pyruvate-labeled. For the exopolysaccharide produced by this strain the following repeating unit has been proposed (Robertsen et al. (1981), Plant Physiol. 67, 389-400): (Formula: see text). The results obtained suggest that the octasaccharide repeating unit (compound a) with one (compound b) or two (compound c) ketal pyruvate residues are assembled on a lipid acceptor. All these compounds are assumed to be intermediates in the biosynthesis of R. trifolii exopolysaccharide.
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PMID:In vitro synthesis of a lipid-linked acetylated and pyruvilated oligosaccharide in Rhizobium trifolii. 394 25

Relapsing fever borreliae require lipid compounds for growth in vitro. In this study, the major pathways of lipid catabolism in three species of tick-borne relapsing fever borreliae were investigated. Thin-layer chromatography was used to compare chloroform-methanol extracts of fresh culture media with extracts of exhausted culture media after organisms were removed by centrifugation. The chromatographic data demonstrated that lysolecithin was removed from the culture media during growth of the spirochetes, whereas lecithin, sphingomyelin, triglycerides, and cholesterol esters were not affected by growth of the organisms. Sonic extracts of the organism were tested for the presence of specific enzymes of lipid catabolism. Lysolecithinase, glycerophosphorylcholine diesterase, and acid phosphatase activities were demonstrated. Thus, these organisms can sequentially dissimilate lysolecithin to fatty acids, choline, inorganic phosphate, and glycerol. Assays for phospholipases A, C, and D, alpha-glycerophosphate dehydrogenase, alkaline phosphatase, and lipase were negative.
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PMID:Lipid catabolism of relapsing fever borreliae. 436 Dec 92

Malondialdehyde, which is generated by lipid peroxidation, can form DNA-protein and/or interstrand DNA crosslinks. The biological consequences of inaccurate repair of these crosslinks may be severe. The expected levels of crosslinking of DNA in vivo are low, and an extremely sensitive method must be used for their detection and measurement. Because both types of crosslinks may contain cytosine, the cytosine residues of DNA were labeled in vitro with 125I. The iodinated DNA was treated with Penicillium nuclease P1 at pH 6 and with alkaline phosphatase at pH 9, and the nucleosidic compounds were analyzed by high-performance liquid chromatography. The optimum conditions for measurement of the crosslinks on Ultrasphere ODS or Zorbax ODS columns were 50 mM ammonium phosphate buffer, pH 7, that contained 2% methanol and 5 mM tetra-t-butylammonium phosphate. Both DNA-protein and interstrand DNA crosslinks were measurable simultaneously. The method was quantitative, reproducible, and able to detect crosslinked adducts at subpicomole levels, so that as few as two crosslinks per 10(6) base pairs were detectable.
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PMID:Detection and measurement by high-performance liquid chromatography of malondialdehyde crosslinks in DNA. 653 42

Brush-border membrane vesicles prepared from rabbit kidney cortex were incubated at 37 degrees C for 30 min with phosphatidylinositol-specific phospholipase C. This maneuver resulted in a release of approx. 85% of the brush-border membrane-linked enzyme alkaline phosphatase as determined by its enzymatic activity. Transport of inorganic [32P]phosphate (100 microM) by the PI-specific phospholipase C-treated brush-border membrane vesicles was measured at 20-22 degrees C in the presence of an inwardly directed 100 mM Na+ gradient. Neither initial uptake rates, as estimated from 10-s uptake values (103.5 +/- 6.8%, n = 7 experiments), nor equilibrium uptake values, measured after 2 h (102 +/- 3.4%) were different from controls (100%). Control and PI-specific phospholipase C-treated brush-border membrane vesicles were extracted with chloroform/methanol to obtain a proteolipid fraction which has been shown to bind Pi with high affinity and specificity (Kessler, R.J., Vaughn, D.A. and Fanestil, D.D. (1982) J. Biol. Chem. 257, 14311-14317). Phosphate binding (at 10 microM Pi) by the extracted proteolipid was measured. No significant difference in binding was observed between the two types of preparations: 31.0 +/- 9.37 in controls and 29.8 +/- 8.3 nmol/mg protein in the proteolipid extracted from PI-specific phospholipase C-treated brush-border membrane vesicles. It appears therefore that alkaline phosphatase activity is essential neither for Pi transport by brush-border membrane vesicles nor for Pi binding by proteolipid extracted from brush-border membrane. These results dissociate alkaline phosphatase activity, but not brush-border membrane vesicle transport of phosphate, from phosphate binding by proteolipid.
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PMID:Enzymatic removal of alkaline phosphatase from renal brush-border membranes. Effect on phosphate transport and on phosphate binding. 669 85

A common method of studying ganglioside metabolism is to measure the amounts of radioactivity incorporated into ganglioside from a radiolabeled precursor. This requires that radioactive nonganglioside material be completely removed from the ganglioside fraction. Nucleotide sugars and aminosugars comprise an important source of such contaminants. Therefore, we have studied their behaviors in several procedures currently employed to isolate gangliosides. Over 50% of the radioactivity associated with several nucleotide sugars added to a brain homogenate is extracted with chloroform/methanol (2:1, v/v), and most of this is recovered in the upper phase of a Folch partition. Dialysis against water removes almost all of the free aminosugar but only 70% of nucleotide sugar. Treatment with alkaline phosphatase, phosphodiesterase and alkaline methanol followed by dialysis removes almost all of the nucleotide diphosphate sugars but only 88% of cytidine 5'-monophosphate sialic acid (CMP-NeuAc). Nucleotide sugars cannot be separated from gangliosides by Unisil or Iatrobead chromatography, but nucleotide diphosphate sugars and gangliosides are resolved with Sephadex LH-20 chromatography following treatment with phosphodiesterase and alkaline phosphatase. CMP-NeuAc was not satisfactorily separated from gangliosides using any of the procedures.
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PMID:Behavior of sugar derivatives in procedures for ganglioside isolation. 674 71


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