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At least 19 recordsLinked to original sources
PubMed2026

Cobalt starvation affects multiple cellular processes in Desulfofundulus kuznetsovii TPOSR during alcohol oxidation.

Cobalt influences the methanol metabolism of Desulfofundulus kuznetsovii TPOSR, specifically by modulating the activity of one of its alcohol dehydrogenases (ADH), Adh1. However, the effects of cobalt on the broader proteome of strain TPOSR, as well as the utilization of alcohols besides methanol, remain unexplored. Here, proteomic analyses of strain TPOSR grown with and without cobalt on different alcohol substrates show that cobalt starvation impacts multiple cellular processes, including cobalamin biosynthesis, iron-sulphur cluster assembly and, most prominently, energy metabolism as indicated by altered abundances of hydrogenases and NAD(P)-dependent oxidoreductases. Despite the presence of six ADH-encoding genes in the genome, Adh1 is the dominant ADH during growth not only on methanol but also on several primary alcohols and diols (ethanol, 1-propanol, 1,2-propanediol, 1,3-propanediol, butanol, pentanol and heptanol). Enzymatic assays with purified Adh1 confirm activity with these substrates, except 1,3-propanediol, and show no activity toward secondary alcohols (2-propanol and 2-butanol). Comparative proteomics analyses of other sulphate-reducing microorganisms (SRMs), namely Desulfofundulus australicum and Solidesulfovibrio carbinolicus, further indicate that methanol and ethanol oxidation in SRMs is mediated by a single ADH/AOR pair. Together, these findings highlight the central role of cobalt in alcohol metabolism in strain TPOSR and identify conserved ADH/AOR enzymes as promising candidates for biotechnological applications.

Cobalt↗
PubMed1977

The role of cytochrome P-450 in the hydroperoxide-catalyzed oxidation of alcohols by rat-liver microsomes.

The organic hydroperoxide cumene hydroperoxide is capable of oxidizing ethanol to acetaldehyde in the presence of either catalase, purified cytochrome P-450 or rat liver microsomes. Other hemoproteins like horseradish peroxidase, cytochrome c or hemoglobin were ineffective. In addition to ethanol, higher alcohols like 1-propanol, 1-butanol and 1-pentanol are also oxidized to their corresponding aldehydes to a lesser extent. Other organic hydroxyperoxides will replace cumene hydroperoxide in oxidizing ethanol but less effectively. The cumene-hydroperoxide-dependent ethanol oxidation in microsomes was inhibited partially by cytochrome P-450 inhibitors but was unaffected by catalase inhibitors. Phenobarbital pretreatment of rats increased the specific activity of the cumene-hydroperoxide-dependent ethanol oxidation per mg of microsomes about seven-fold. The evidence suggests that cytochrome P-450 rather than catalase is the enzyme responsible for hydroperoxide-dependent ethanol oxidation. However, when H2O2 is used in place of cumene hydroperoxide, the microsomal ethanol oxidation closely resembles the catalase system.

Alcohols↗
PubMed1979

Alcohol-induced switching over of metabolic flux in Streptomyces noursei JA0 3890b.

Short-chain alcohols, benzyl alcohol and Tween 20 were found capable of switching over the metabolic flux in Streptomyces noursei JA 3890b from the preference of oxidative deamination of alanine towards the reinforced acquisition of NH4+. These changes were correlated to the decrease of the ratio of saturated to olefinic fatty acids in the mycelium, suggesting that alcohols and other polar lipophilic compounds can interfere with the biosynthesis and the function of the cytoplasmic membrane in Streptomyces.

1-Propanol↗
PubMed1975

A comparative study on the irreversible binding of labeled halothane trichlorofluoromethane, chloroform, and carbon tetrachloride to hepatic protein and lipids in vitro and in vivo.

1) After intraperitoneal injection of labeled CCl4, CHCl3, and halothane in mice, 14C is preferentially bound to liver endoplasmic protein and lipid. A considerable activity is also associated with mitochondrial constituents. Maximal protein binding (nmol/mg): CCl4: 2.8 (0.5 hrs); CHCl3: 11.5 (6 hrs); halothane: 5 (6 hrs). Lipid binding: CCl4: 6.4 (5 min); CHCl3: 8 (4 hrs); halothane: 13.5 (2 hrs). The form of the binding curves in microsomal and mitochondrial protein and lipid differed with the individual haloalkanes. 2) The irreversible (covalent) binding of 14C from labeled haloalkanes in anaerobic suspensions of isolated rabbit liver microsomes and NADPH after 30 min was for protein (lipid) (nmol/mg): CCl4: 15 (58); CHCl3: 3.4 (3.2); halothane: 2.3 (10); trichlorofluoromethane: 6.5 (30). Anerobic incubation favored dehalogenation, but CHCl3 metabolism and irreversible binding requires oxygen. The greatest differences in the in vitro "covalent" binding rates were observed with CHCl3 in rat, mouse, and rabbit. 3) Altered microsomal cytochrome P-450 concentrations in newborn animals, or produced by pretreatment of rats with phenobarbital, 3-methylcholanthrene (MC), or CoCl2 effected similar, but not proportional changes in the rates of irreversible protein and lipid binding. Upon addition of CCl4 the difference of light absorption of reduced liver microsomes from MC-pretreated rats containing cytochrome P-448 appeared at 452 nm. The irreversible binding rate in these microsomes was also increased. The small accleration in irreversible binding in liver microsomes from rats pretreated with isopropanol is not proportional to the high increase of CCl4 toxicity. 4) Practically no binding to added, soluble albumin or RNA was observed in microsomal incubates. However, 14C is bound to the nicotine-adenine dinucleotides of the NADPH system. All haloalkanes produced a similar increase of NADPH oxidation in incubates of rabbit liver microsomes and NADPH.

1-Propanol↗
PubMed1978

On the synthesis of serine and homoserine samples asymmetrically labelled with tritium and deuterium in the hydroxymethylene group.

(1R) [1-3H, 2H1] 3-Phenylpropanol, the key intermediate in the synthesis of (4R) [4-3H, 2H1] D,L-homoserine and of the (4S)-isomer, is obtained from (1S) [1-2H1] 3-phenylpropanol and (1RS) [1-3H] ethanol upon incubation with yeast alcohol dehydrogenase and NAD+; under similar conditions 2-phenylethanol undergoes very small exchange with [1-2H2] ethanol.

1-Propanol↗
PubMed1977

Effect of alcohols on the structure and function of D-amino-acid oxidase.

The absorption spectrum of D-amino-acid oxidase (D-amino-acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3) was significantly perturbed by various alcohols; typical fine structures were observed in the visible absorption bands, accompanied by blue shifts of the peaks. Both fluorescence intensity and fluorescence polarization were increased upon the addition of alcohols, indicating that the coenzyme is not liberated from the apoenzyme but the hydrophobicity of the environment of the enzyme-bound flavin is increased. Upon the addition of alcohols, the circular dichroism of the enzyme was markedly modified in the visible and near-ultraviolet regions, while that of the apoenzyme in the near- and far-ultraviolet regions was scarcely modified, indicating a change in the interaction between the flavin coenzyme and protein. Both the apparent maximal velocity and the apparent Michaelis constant of the enzyme were increased by the addition of alcohols. The presence of alcohols tends to dissociate the dimer of this enzyme into the monomer, but the dissociation does not fully explain the increase in the maximal velocity of the enzyme by alcohols, because the increase in the maximal velocity caused by alcohols is larger than that expected from the dissociation. Since the rate of formation of the purple intermediate was decreased by alcohols in both the dimer and the monomer, the increase in the maximal velocity could be ascribed to an increase in the rate of dissociation of the enzyme-product complex. This increase could be ascribed to the protein conformational change, which is probably provoked by combination of alcohols with the enzyme at a locus other than that for substrate binding.

1-Propanol↗
PubMed1979

Mutagenic activation of tris(2,3-dibromopropyl)phosphate: the role of microsomal oxidative metabolism.

The flame retardant tris(2,3-dibromopropyl)phosphate (Tris-BP) is converted to products which are mutagenic for Salmonella typhimurium TA 100 in the presence of rat liver microsomes, NADPH and oxygen. Other bromopropyl-compounds were also mutagenic; 2,3-dibromopropene and 2,3-dibromopropionic acid were directly mutagenic, whereas 2,3-dibromopropanol and tris(2-bromopropyl)phosphate were weakly mutagenic after addition of liver microsomes and cofactors. Typical in vivo and in vitro inhibitors of cytochrome P-450 inhibited Tris-BP mutagenicity. The effects of inducers of cytochrome P-450 on Tris-BP mutagenicity was dependent on the concentration of mutagen and microsomal protein in the assay, indicating complexity in the kinetics involved when dealing with possible multiple pathways that lead to mutagenicity. Addition of glutathione strongly inhibited Tris-BP mutagenicity. It is suggested that Tris-BP is oxidized to a reactive electrophile, possibly the 2-keto derivative, which could react with nucleophilic groups in DNA and thus lead to mutagenic events.

1-Propanol↗
PubMed1977

The effect of compression on some physical properties of microcrystalline cellulose powders.

Tablets have been prepared from previously characterized microcrystalline cellulose (Avicel) powders, using an instrumented single station tablet machine. The regenerated particle size was found to increase in compaction pressure. Compaction caused a slight initial decrease in B.E.T. surface area, followed by an increase mainly as a result of elastic recovery of the particles. The intra-particulate pore size distribution showed no change throughout the range of compaction pressures studied, demonstrating that the internal pores did not collapse. Measurement of the interparticulate porosity by mercury porosimetry, liquid penetration techniques and scanning electron microscopy showed a decrease in this parameter with increase in compaction pressure. The dissolution behaviour from the compacts showed in general a decreased rate with increase in compaction pressure, that from the cellulose grade PH 105 being slower than from the remaining grades.

1-Propanol↗
PubMed1975

Determination of sulfur trioxide in engine exhaust.

Sulfur trioxide in the exhaust gas of an internal combustion engine is removed and concentrated by absorption in a solution of 80% isopropyl alcohol, which quantitatively absorbs it and inhibits the oxidation of any sulfur dioxide which may be absorbed. The absorbed sulfur trioxide (sulfuric acid) is determined by an absorption titration by using barium chloride as the titrant and thorin as the indicator. The sulfur dioxide content of the exhaust is measured continuously by means of a DuPont Model 411 ultraviolet photoanalyzer.

1-Propanol↗
PubMed1975

Elimination of precipitates in oil red O fat stain by adding dextrin.

Addition of dextrin in the final 60% isopropanol of the Lillie-Ashburn super-saturated oil red O isopropanol technic moderately intensified the stain and decreased our required staining interval. Precipitates were decreased and the diluted solution remained usable into the second week. A saturated 60% isopropanol oil red O solution contained 33 mg/100 ml. Without dextrin the fresh supersaturated solution contains 40 mg, after 3 days 25 mg. With dextrin the fresh solution contained 130 mg dye, the 10-day-old one 100 mg/100 ml.

1-Propanol↗
PubMed1975

[Action of isopropanol on rat lipid metabolism: complementary studies on mechanisms implicated in hepatic accumulation of triacylglycerides].

Isopropanol administration (3 g/kg, p.o.) determines in the rat liver an inhibition of fatty acid oxidation, an enhancement of fatty acid esterification into triacylglycerols as well as an inhibition of lipoprotein secretion which appears to be related to alterations in hepatic phospholipids and which differentiates isopropanol from ethanol induced fatty liver. Disturbances in peripheral lipolysis following isopropanol administration are found only in mature rats and are not necessary to the fatty liver induction.

1-Propanol↗
PubMed1976

Human epidermal transglutaminase. Preparation and properties.

A transglutaminase from human hair follicle-free epidermis was purified to homogeneity using gel filtration and ion exchange chromatography. The enzyme had an apparent Mr = 51,000 +/- 2,000 by sodium dodecyl sulfate electrophoresis, 100,000 +/- 5,000 by discontinuous gel electrophoresis, and 50,000 +/- 2,000 by gel filtration in Bio-Gel A-0.5m agarose. The enzyme cross-linked Factor XIII-free fibrinogen forming gamma dimers and alpha polymers. Either calcium or strontium was necessary for enzyme activity. In the presence of calcium, enzyme activity was increased by heating at 56 degrees or by treating with dimethylsulfoxide. Activation required calcium and occurred in the presence of serine protease inhibitors. The activated and native enzyme had apparently identical mobilities in acrylamide disc electrophoresis and sodium dodecyl sulfate electrophoresis. The Km values for two substrates in the reaction, casein and putrescine, were very similar for the native and the activated enzyme. The activated enzyme had a larger elution volume on Bio-Gel A-0.5m in the presence of calcium than did the native enzyme. The detailed mechanism of activation remains to be determined.

1-Propanol↗
PubMed1976

[Sterilization of intratracheal tubes].

After a brief review of classical and modern methods of sterilisation of endo-tracheal catheters, where they emphasize the dangers of the use of ethylene oxide, the authors recall the common procedure which they used: washing with water and soap, and soaking for 6 to 7 hours in formaldehyde or in a solution of quaternary ammonium salts, and all manipulations should be made using gloves.

1-Propanol↗
PubMed1976

Interaction of adrenergic antagonists with prostaglandin E2 and tetrahydrocannabinol in the eye.

Both alpha- and beta-adrenergic antagonists have been utilized in an atempt to discern the site of action of prostaglandin (PG) and tetrahydrocannabinol (THC) in the eye. Both alpha- and beta-adrenergic antagonists (alpha-antagonists, phentolamine and phenoxybenzamine; beta-antagonists, propranolol and sotalol) cuased a dose-dependent reduction in intraocular pressure and blood pressure and increased total outflow facility. The results are consistent with the concept that both alpha- and beta-adrenergic receptors are present in the anterior uvea and that vasomotor tone is essential to the maintenance of normal intraocular pressure. No antagonist reduced the PG-induced elevation of intraocular pressure unless the blood pressure was severely lowered. All antagonists inhibit the normal PG-induced increase in total outflow facility, indicating that these agents protect the blood-aqueous barrier from breakdown without altering the vasodilatory response to PG. All antagonists reduced the fall in intraocular pressure produced by THC by approximately 50 per cent, except for sotalol which completely abolished the intraocular pressure fall. Only the alpha-adrenergic antagonists prevented the THC-induced increase in total outflow facility. The results indicate that true outflow facility may well be regulated exclusively by alpha-receptors. The data are consistent with the effect of THC being primarily a vasodilation of the efferent blood vessels of the anterior uvea. The partial inhibition by alpha-adrenergic antagonists may also suggest a lesser role of THC on the afferent vessels.

1-Propanol↗