Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: KEGG:D06522 (Silica)
 2,396 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A sensitive and convenient radioassay for the in vitro determination of ethylmorphine N-demethylase and O-de-ethylase activity has been developed. Ethylmorphine[6-3H] was prepared by reduction of the corresponding morphinone in nearly quantitative yield. After incubation with hepatic microsomes from male rats, the reaction was terminated by the addition of 5 ml of acetone. The sample was saturated with potassium acetate and extracted twice with acetone giving complete extraction of the radiolabeled ethylmorphine and its metabolites. After the combined organic phases were evaporated, the samples were dissolved in methanol and applied to a Silica Gel GF plate with subsequent development in ethyl acetate-methanol-concentrated NH4OH. The amount of radioactivity detected for the morphine and norethylmorphine bands at zero time was approximately 0.05% of the original amount of labeled ethylmorphine added to the incubation media. Similarly, the Km values were 52 and 250 microns for the O- and N-dealkylation respectively, while the Vmax values were 5.0 and 1.8 nmol/mg of protein per min. Finally, with this assay we have observed constant specific activity for both the N- and O-dealkylation of ethylmorphine[6-3H] with as little as 10 micrograms of microsomal protein per ml of incubation media.
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PMID:Studies on the N-demethylation and O-de-ethylation of ethylmorphine[6-3H] by male rat hepatic microsomes. 49 Mar 20

26,27-Oxido-5 alpha-cholestane-3 alpha,7 alpha,12 alpha-triol can be obtained in a homogeneous state in gram quantities by passing it through one PrepPak-500/Silica cartridge mounted in a Waters Assoc. preparative liquid chromatograph. The elution solvent was methanol-chloroform (1:14). The isolated material was analyzed for purity by several chromatographic means and by elemental analysis, and was finally characterized by the usual spectroscopic means. Gas-liquid chromatography of its trimethylsilyl ether indicated the formation of a tetrakis-trimethylsilyl-26-chloro derivative, in addition to the expected tris-trimethylsilylated substance. The structure of the former compound is deduced from the fragmentation and isotope abundance in its mass spectrum and from chemical principles.
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PMID:Bile acids. LIX. Purification of 5 alpha-anhydrocyprinol by preparative high-performance liquid chromatography. 57 15

An effective resolution of intact phosphatidylserines on the basis of unsaturation has been achieved by conventional argentation thin layer chromatography (TLC) following trifluoracetylaction. The trifluoroacetamides are prepared by treatment with trifluoroacetic anhydride or N-methyl-bis-trifluoroacetamide. The acetamides are resolved with chloroform-methanol-water (65:25:4, v/v/v) on Silica Gel G containing 20% silver nitrate. Subfractions with 0-6 double bonds per molecule were obtained for the phosphatidylserines of pig and ox brain, pig erythrocytes, rat liver, and rabbit skeletal muscle. The preparation of trifluoroacetamides is also advantageous for the silver ion fractionation of phosphatidylethanolamines. The method is applicable to metabolic studies of molecular species using radioactive precursors of neutral lipids, phosphorus, and nitrogenous bases.
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PMID:Resolution of molecular species of intact serine and ethanolamine phosphatides by argentation chromatography of their trifluoroacetamides. 89

1. Subcellular fractions isolated from livers of 19-day-old chicken embryos were analyzed in order to assess whether liver mitochondria contained glycosylated proteins or had mannosyl- or sialyl-transferases that could transfer sugars to mitochondrial macromolecules. 2. Proteins in liver mitochondrial membranes and matrix fractions were screened for their affinities for concanavalin A (Con A). 3. After separation by gel electrophoresis under denaturing conditions, a significant number of the proteins bound [125I]Con A, and the binding of the lectin was substantially inhibited by alpha-methyl-D-mannoside. 4. In addition, radio-iodinated matrix proteins were screened for lectin-binding properties by chromatography on Con A covalently linked to agarose. 5. A number of proteins, representing 14% of those loaded onto the column, became tightly bound to the agarose-linked lectin, and the molecular weights of several of those proteins are reported. 6. Mannosyltransferase activities were measured in fractions highly enriched for mitochondria. 7. In the reactions, mannose was transferred from guanosine diphosphomannose to materials insoluble in 0.3% trichloroacetic acid or in chloroform:methanol (2:1). 8. The fractions also catalyzed the transfer of mannose to materials extractable in chloroform:methanol and which migrated with the Rf of dolichol phosphate on Silica Gel H. 9. Dolichol phosphate stimulated the transfer of mannose to those materials extractable in the organic solvents. 10. Marker enzyme analyses indicated that the mannosyl transferase activity in the mitochondrial fraction could not be accounted for entirely by contaminating microsomal membranes. 11. Although sialyltransferase activity was detected also in the mitochondrial fractions, the levels of the activity and the kinetics of the reactions indicated that Golgi membranes were most likely the sources of the enzyme.
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PMID:Mitochondrial biogenesis: do liver mitochondria contain glycoproteins and glycosyltransferases? 228 16

A rapid and accurate assay for lipase-catalyzed hydrolysis of radioactively labeled triacylglycerols has been developed. Aliquots of reaction mixtures are applied directly, i.e., without extraction of the lipolysis products, to thin-layer chromatography plates coated with Silica Gel H containing 5% Na2CO3 (w/w), heated for 10 sec, and developed with diethyl ether-methanol 97:3 (v/v) to a height of 4-5 cm. About 98.5% of the fatty acids are immobilized as sodium salts at the origin of the chromatogram, whereas tri-, di-, and monoacylglycerols migrate close to the solvent front. Adsorbent at the origin and that at the remaining part of the chromatogram are then assayed for radioactivity without prior staining.
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PMID:Assay for triacylglycerol lipase by a rapid thin-layer chromatographic technique. 323 22

The major complement-fixing antigen of Mycoplasma pneumoniae is found in the lipid fraction of the organism. When the lipids of M. pneumoniae were fractionated by column chromatography on silicic acid, serological activity against both rabbit and human immune sera was found in two fractions, B and D. Fraction B, eluted with chloroform-methanol (9:1), was a minor component in terms of total complement-fixing activity and contained a complex of lipids which were detected in the region characteristic of phosphatidic acids by thin-layer chromatography on Silica Gel G. Fraction D, eluted with ethyl acetate-methanol (3.5:2), had approximately the same complement-fixing antigen titer as the original lipid extract and appeared as a "comet-shaped" spot between phosphatidylethanolamine and phosphatidylcholine on Silica Gel G plates charred with sulfuric acid. However, by thin-layer chromatography on Silica Gel H impregnated with sodium tetraborate, it was demonstrated that fraction D did contain multiple components, all but one of which were carbohydrate-containing lipids (giving positive reactions when sprayed with orcinol-sulfuric acid reagent). Fraction D was found to contain glycerol and phosphate in equimolar ratios but did not contain nitrogen. Two sugars were detected which migrated on paper chromatograms with glucose and galactose.
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PMID:Immunochemical analysis of serologically active lipids of Mycoplasma pneumoniae. 568 95

After the intraportal injection of retinoic acid-15-(14)C into rats, all-trans methyl retinoate, a cis isomer of methyl retinoate, retinoyl beta-glucurono-gamma-lactone, retinoic acid, and retinoyl beta-glucuronide were isolated from methanol extracts of rat bile by chromatography on anion-exchange resin and silicic acid columns and characterized on thin-layer plates of Silica Gel G. On the other hand, when bile was extracted with n-butanol or analyzed directly by thin-layer chromatography, only retinoyl beta-glucuronide and a very small amount of retinoic acid could be detected. Butanol extracts of the liver and the intestine, however, still contained a small radioactive nonpolar fraction. When retinoyl beta-glucuronide was incubated with an anion-exchange resin in the presence of methanol, several nonpolar products appeared. Apparently the methyl retinoate, retinoyl beta-glucurono-gamma-lactone, and most of the retinoic acid previously found in bile after retinoic acid administration are produced from retinoyl beta-glucuronide during the isolation procedure.
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PMID:Origin of some derivatives of retinoic acid found in rat bile. 572 16

Gluco- and galactocerebrosides can be separated by thin-layer chromatography on Silica Gel G prepared with sodium borate solution instead of water. The most successful developing system was chloroform-methanol-water-15 M NH(4)OH 280:70:6:1.
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PMID:Separation of gluco- and galactocerebrosides by means of borate thin-layer chromatography. 592 60

A sulfoglycosphingolipid containing N-acetylgalactosamine has been isolated from the lipid extract of rat kidney. The isolation procedure involved extraction of lipids with chloroform/methanol, alkaline methanolysis, and column chromatographies with DEAE-Sephadex and Silica beads. The components were N-acetylgalactosamine, galactose, glucose, sphingoid bases, fatty acids, and sulfate in equimolar amounts. The yield of this sulfoglycolipid was about 24 nmol/g of tissue, which was about 13% of that of galactosylceramide 3-sulfate from rat kidney. By infrared spectroscopy, proton magnetic resonance spectroscopy, periodate oxidation, solvolysis, chromium trioxide oxidation, and methylation analysis of the native and partially degraded compound, the structure of this glycolipid is proposed to be GalNAc beta 1--4(HSO3-3)Gal beta 1--4Glc beta 1--1Cer.
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PMID:Isolation and characterization of the sulfated gangliotriaosylceramide from rat kidney. 705 29

Enzymatic step-wise methylation of membrane phosphatidylethanolamine (PE) to phosphatidyl-N-methylethanolamine (PME) and then phosphatidyl-choline (PC) has been known to alter membrane properties and responsiveness of cells for activation of receptors by chemical transmitters. Conversion of PE to PME and PME to PC in the presence of S-adenosyl-L-methionine (SAM) are catalyzed by two phospholipid N-methyltransferases, PMT I and PMT II, of which PMT I is the rate limiting enzyme. Retina is a good neuronal model for chemical transmission. However, retina was not studied for PMT activity. Therefore, we studied the rat retina for PMT I activity. Methylation of PE in the rat retinal sonicates was assayed using 3H-SAM (2 microM) at 37 degrees C in Tris-glycylglycine buffer (50 mM, pH 8.0) and methylated phospholipids were extracted with chloroform/methanol/HCl (2/1/0.02, v/v) and separated by thin layer chromatography on Silica Gel G plates. Chromatograms were developed in a solvent system of propionic acid/n-propyl alcohol/chloroform/water (2/2/1/1, v/v). This study gave the following results: (a) the total methylated phospholipids were (M +/- SE, N = 5) 19.90 +/- 4.03 fmol/mg protein/min; (b) the major methylated phospholipid was PME (4.21 +/- 0.68 fmol/mg protein/min; (c) the fatty acid methylesters formed by fatty acid carboxymethylase (FACM) which accumulated in the solvent front amounted to 18.82 +/- 2.84 fmol/mg protein/min. Both PMT I and FACM were inhibited by S-adenosyl-L-homocysteine (I50, 1.2-5 microM). These observations indicate that rat retina contains both PMTs and FACM.
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PMID:S-adenosyl-L-methionine-mediated enzymatic methylations in the rat retinal membranes. 820 29


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