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At least 271 records · Page 15Linked to original sources
PubMed1983

[Submergence of Micrococcus lysodeikticus F1-ATPase into the hydrophobic phase of the membrane, using 2,4,6-trinitrobenzosulfonate and 12-0-(azidoformyl) stearic acid methyl ester].

The accessibility of F1-ATPase from Micrococcus lysodeikticus in solution and in the membrane for the specific water-soluble NH2-group reagent, 2,4,6-trinitrobenzosulfonate (TNBS), was studied. Incubation of the soluble factor F1 with 50 mM TNBS pH 8.3 results in incorporation of 58.6 +/- 4.4 trinitrophenyl residues per mole of enzyme. At the same time F1-ATPase isolated from TNBS-pretreated membranes contains 27.2 +/- 2.0 TNP-residues per mole of enzyme. It is assumed that the different accessibility of F1-ATPase for TNBS in solution and in the membrane is due to incorporation of F1-ATPase into the membrane. Study of membrane F1-ATPase interaction with the radioactive lipid-soluble photoreactive label, 12-0-(azidoformyl) stearic acid methyl ester demonstrated that F1-ATPase does not immediately interact with the lipid phase of the membrane. It is suggested that membrane F1-ATPase may be enveloped by hydrophobic proteins.

Affinity Labels↗
PubMed2003

Stearic acid stimulates FA ethyl ester synthesis in HepG2 cells exposed to ethanol.

FA ethyl esters (FAEE) are nonoxidative metabolites of ethanol produced by the esterification of FA and ethanol. FAEE have been implicated as mediators of ethanol-induced organ damage in vivo and in vitro, and are markers of ethanol intake. Upon ethanol intake, FAEE are synthesized in the liver and pancreas in significant quantities. There is limited information on the stimulation of FAEE synthesis upon addition of exogenous FA in vitro. HepG2 cells were incubated with ethanol alone, ethanol with 25 microM linoleate, and ethanol with 25 microM stearate. The amount of FAEE in human hepatoblastoma (HepG2) cells was determined 1-3 h after ethanol and FA addition. Stearate increased the FAEE concentration in HepG2 cells when incubated with the cells for 1 h, whereas linoleate did not increase the cellular FAEE concentration at any time. Ethyl palmitate, ethyl stearate, and ethyl oleate were the predominant FAEE species identified in all cases, independent of the specific supplemental FA added to the medium.

Carcinoma, Hepatocellular↗
PubMed1999

An investigation into the release of cefuroxime axetil from taste-masked stearic acid microspheres. Part 1: the influence of the dissolution medium on the drug release profile and the physical integrity of the microspheres.

The dissolution properties of stearic acid-coated cefuroxime axetil (SACA) systems have been studied with a view to investigating the effects of the dissolution medium on both the release rate and the physical integrity of the microspheres. The release from the spheres was found to be highly dependent on the media used, with systems in distilled water (pH 6.8) and pH 5.9 Sorensens modified buffer showing a relatively slow release which exhibited linearity with the square root of time, implying a diffusion process. The rate of release from systems in pH 7.0 and 8.0 buffer was considerably faster and did not follow simple diffusion kinetics. Examination of the microspheres after immersion in the various media indicated a change in the integrity of the spheres in those media which showed the most rapid release. This was particularly marked when the systems were dried in buffer, with disintegration seen in the higher pH systems. It is suggested that the release of the drug is dependent both on diffusion through the intact microspheres and changes in the physical integrity of the spheres as a result of a reaction with the surrounding medium.

Cefuroxime↗
PubMed1979

Factors regulating the elongation of palmitic and stearic acid by rat liver microsomes.

Analysis of the rates of overall chain elongation and condensation of malonyl-CoA with palmitoyl-CoA and stearoyl-CoA as primers demonstrated that for each primer, the rate of the overall metabolic process was similar to the initial condensation. The specific activity for condensation with palmitoyl-CoA was eleven times greater than for stearoyl-CoA. The specific activities of both the beta-hydroxyacyl-CoA dehydrase and 2-trans-enoyl-CoA reductase reactions were much higher than for either condensation or chain elongation, although these rates were somewhat greater with the intermediates required in chain elongating palmitoyl-CoA than for stearoyl-CoA. Both substrates were incorporated into phospholipids at low rates and there was a time-dependent hydrolytic cleavage of the acyl-CoA primers which was partially prevented by bovine serum albumin. These findings demonstrate that there was no selective removal of either primer which could result in specific substrate depletion and an apparent reduction in the rate of condensation. These combined results firmly establish the rate-limiting nature and high degree of substrate specificity exhibited during the initial condensation step in fatty acid elongation.

Animals↗