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Results for “Chloroquinolinols”

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At least 19 recordsLinked to original sources

Sulfate transport mechanisms in epithelial systems.

A novel invertebrate gastrointestinal transport mechanism has been shown to couple chloride-sulfate exchange in an electrogenic fashion. In the lobster, Homarus americanus, the hepatopancreas, or digestive gland, exists as an outpocketing of the digestive tract, representing a single cell layer separating the gut lumen and an open circulatory system composed of hemolymph. Investigations utilizing independently prepared brush border and basolateral membrane vesicles revealed discrete antiport systems which possess the capacity to bring about a transcellular secretion of sulfate. The luminal antiport system functions as a high-affinity, one-to-one chloride-sulfate exchanger that is stimulated by an increase in luminal hydrogen ion concentration. Such a system would take advantage of the high chloride concentration of ingested seawater as well as the high proton concentrations generated during digestion, which further suggests a potential regulation by resident sodium-proton exchangers. Exchange of one chloride for one divalent sulfate ion provides the driving force for electrogenic vectorial translocation. The basolateral antiport system was found to be electroneutral in nature, responsive to gradients of the dicarboxylic anion oxalate while lacking in proton stimulation. No evidence of sodium-sulfate co-transport, commonly reported for the brush border of vertebrate renal and intestinal epithelia, was observed in either membrane preparation. The two antiporters together can account for the low hemolymph to seawater sulfate levels previously described in decapod crustaceans. A secretory pathway for sulfate based upon electrogenic chloride-antiport may appear among invertebrates partly in response to digestion taking place in a seawater environment. J. Exp. Zool. 289:245-253, 2001.

Animals↗

Reverse-phase high-performance liquid chromatographic determination of halogenated 8-hydroxyquinoline compounds in pharmaceuticals and bulk drugs.

A reverse-phase high-performance liquid chromatographic (HPLC) method was developed for determining iodochlorhydroxyquin, 5,7-dichloro-8-hydroxyquinoline, and 5,7-diiodo-8-hydroxyquinoline in creams, ointments, shampoos, tablets, and bulk drugs. A column packed with 10-micron phenyl-silica and a mobile phase of 0.001 M NiCl2 in acetonitrile-methanol-water (30:20:50) was used to separate the nickel complexes of the three drugs, with detection at 273 nm. Analysis of creams, ointments, shampoos, and tablets gave results close to the label declarations. Recovery of standard material added to samples was greater than or equal to 98%. Linearity of response was shown over a range of 30-150% of label claim for standards of the three drug substances. Multiple analyses of iodochlorhydroxyquin and diiodohydroxyquinoline bulk drugs showed purities of 99.96 and 98.77% with CV of 1.17 and 0.73%, respectively. The HPLC method offers an alternative to current USP procedures, which lack stability-indicating and specificity characteristics.

Chloroquinolinols↗

Fluorimetric determination of chloroxine using manual and flow-injection methods.

A reliable and highly sensitive method is described for the determination of chloroxine in pharmaceutical preparations. It involves the formation of a complex between chloroxine and aluminum(III) in a micellar medium. The complex is a very fluorescent species, and there is a linear relationship between chloroxine concentration and fluorescence intensity over the range 2.0 x 10(-8)-5.1 x 10(-5) mol l-1. The limit of detection is 5 x 10(-9) mol l-1. The method can be easily adapted to a flow system using a three-channel manifold, the peak height being proportional to the chloroxine concentration over the range 5.6 x 10(-7)-5.6 x 10(-5) mol l-1. Manual and flow-injection procedures permit the determination of chloroxine in the presence of chlorquinaldol, and have been successfully applied to the determination of chloroxine in pharmaceutical preparations.

Aluminum↗

New antifungal agents that inhibit the growth of Candida species: dichlorinated 8-quinolinols.

Five dichlorinated 8-quinolinols (2,5- 5,6-, 3,5-, 3,7-, and 4,5-dichloro-8-quinolinol) were tested against Candida albicans and C. tropicalis in Sabouraud dextrose broth with and without bovine serum. The 5,6-, 3,5-, and 3,7-dichloro-8-quinolinols proved to be more effective than the control, 5-fluorocytosine. In cytotoxicity tests employing baby hamster kidney (BHK) cells, all test agents proved to be more cytotoxic than the control. However, the minimum inhibitory concentration (MIC) of 3,5-dichloro-8-quinolinol to both fungi was only one tenth the cytotoxic dose, suggesting that the compound may be useful as a topical or systemic antifungal agent.

Animals↗

A monooxygenase catalyzes sequential dechlorinations of 2,4,6-trichlorophenol by oxidative and hydrolytic reactions.

Ralstonia eutropha JMP134 2,4,6-trichlorophenol (2,4,6-TCP) 4-monooxygenase catalyzes sequential dechlorinations of 2,4,6-TCP to 6-chlorohydroxyquinol. Although 2,6-dichlorohydroxyquinol is a logical metabolic intermediate, the enzyme hardly uses it as a substrate, implying it may not be a true intermediate. Evidence is provided to support the proposition that the monooxygenase oxidized 2,4,6-TCP to 2,6-dichloroquinone that remained with the enzyme and got hydrolyzed to 2-chlorohydroxyquinone, which was chemically reduced by ascorbate and NADH to 6-chlorohydroxyquinol. When the monooxygenase oxidized 2,6-dichlorophenol, the product was 2,6-dichloroquinol, which was not further converted to 6-chlorohydroxyquinol, implying that the enzyme only converts 2,6-dichloroquinone to 6-chlorohydroxyquinol. Stoichiometric analysis indicated the consumption of one O2 molecule per 2,4,6-TCP converted to 6-chlorohydroxyquinol, ruling out the possibility of two oxidative reactions. Experiments with 18O-labeling gave direct evidence for the incorporation of oxygen from both O2 and H2O into the produced 6-chlorohydroxyquinol. A monooxygenase that catalyzes hydroxylation by both oxidative and hydrolytic reactions has not been reported to date. The ability of the enzyme to perform two types of reactions is not due to the presence of a second functional domain but rather is due to catalytic promiscuity, as a homologous monooxygenase converts 2,4,6-TCP to only 2,6-dichloroquinol. Employing both conventional catalysis and catalytic promiscuity of a single enzyme in two consecutive steps of a metabolic pathway has been unknown previously.

Catalysis↗

Contact dermatitis in animal feed mill workers.

Three cases of contact dermatitis due to additives in animal feed substances are described occurring in animal feed workers. There were two cases of sensitivity to ethoxyquin and one to halquinol.

Adult↗

A study of fluctuations in Escherichia coli sensitivity patterns from pigs fed a halquinol supplemented diet.

Escherichia coli isolated from pigs fed on a medicated diet containing 120 p.p.m. halquinol did not develop any resistance to this addition over a 6-week period. Sensitivity patterns of the E. coli isolates to eight antimicrobial substances, although fluctuating slightly during the test period (but no more than a control group), did not significantly alter. However, the patterns did change significantly when for 17 days after the completion of the halquinol trial the pigs were fed a normal commercial ration medicated with a commonly used feed additive containing chlortetracycline hydrochloride, procaine penicillin and sulphadimidine.

Animals↗