<i>Pseudomonas aeruginosa</i>and the general hospital: a six-year survey

Harris, D. M.; Gray, Peter B.

doi:10.1017/s0022172400024098

Cited by 8 publications

(6 citation statements)

References 13 publications

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“…aeruginosa, like other gramnegative organisms, is not generally found on normal skin, although it may appear as a transient organism in moist areas (Lowbury, 1969;Grogan, 1966). The establishment of this organism on the skin is, however, affected by the presence of tissue damage (Lowbury & Fox, 1954;Harris & Gray, 1974). Results from the present study appear to support this in that most of the bedsores were infected with Ps.…”

Section: Discussionsupporting

confidence: 66%

Microbial contamination of topical medicaments used in the treatment and prevention of pressure sores

Baird

Farwell

Sturgiss

et al. 1979

J. Hyg.

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Section: Discussionsupporting

confidence: 66%

Microbial contamination of topical medicaments used in the treatment and prevention of pressure sores

Baird

Farwell

Sturgiss

et al. 1979

J. Hyg.

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“…For an estimation of the correlation time ~' c we can use If the alcohols are bound to lipoxygenase, their rotational correlation time ~'R can be taken as that of the whole protein molecule and can be esti- [19][20][21] and, hence, does not contribute to the correlation time. Preliminary T~ measurements on samples prepared as described in Fig.…”

Section: Resultsmentioning

confidence: 99%

1H-NMR spectroscopic study on the binding of alcohols to soybean lipoxygenase-1

Slappendel

Aasa

Falk

et al. 1982

Biochimica et Biophysica Acta (BBA) - Protein Structure and Mol

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The line-shape of the EPR signal around g 6 of yellow lipoxygenase-l, obtained upon addition of I molar equivalent of 13-Ls-hydroperoxy-9-cis, ll-trans-octadecadienoic acid to the native enzyme (linoleate:oxygen oxidoreductase, EC 1.13.11.12), is strongly affected by alcohols. NMR spectra of solutions of alcohols to which lipoxygenase has been added show a line-broadening of the proton resonances which is due to proton relaxation enhancement from magnetic interaction between iron and protons. This can be taken as direct evidence for binding of alcohols in the vicinity of iron. For unbranched alcohols the line-broadening gradually increases, going from the methyl protons to the protons on carbon atom I, indicating that the latter are closer to iron. Titrations of yellow lipoxygenase with ethanol, 1-butanol and l-bexanol reveal that the affinity of the alcohols increases with longer carbon chain length; their binding constants were found to be 260, 30 and approx. 3 mM, respectively. The distances between protons of bound alcohol and iron were calculated with the Solomon-Bloembergen equation, leading to values of approx. 6 h, for the distance between iron and the methyl protons. A hydrophobic binding of the alcohols to the enzyme is proposed in line with the mode of binding of the natural substrates, polyunsaturated fatty acids.

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“…Carbonate, or possibly bicarbonate (17), is the anion preferred by the protein, but when all hydrated forms of carbon dioxide are excluded from solution, a number of other anions may also activate the metal-binding sites. These include, but are not limited to, oxalate, malonate, thioglycollate, glycinate, EDTA, and possibly citrate (16,18,19).…”

Section: Properties Of Serum Transferrinmentioning

confidence: 99%

Transport of Iron by Transferrin

Aisen

Leibman

1977

Advances in Chemistry

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Transferrin provides iron for the biosynthesis of hemoglobin and probably also for other essential iron proteins. Both active sites bind iron tightly enough to resist hydrolysis but reversibly so that the protein undergoes many cycles of iron transport. These sites do not exist unless a stereochemically suitable anion is available to stabilize them, probably acting as a bridging ligand between metal and protein. The initial event in iron delivery by transferrin to hemoglobin-synthe sizing red blood cells is protein binding to specific receptors on the cell membrane surface. In the rabbit, this receptor appears to be a glycoprotein. After binding, iron may be released from transferrin to the cell by attack on the stabi lizing anion. The protein is then returned to the circulation for another cycle of iron transport. TTnder the conditions found in most biologic fluids, iron is readily^ oxidized by molecular oxygen to the ferric state. Ferric iron, how ever, is prone to hydrolyze, forming insoluble polynuclear ferric hydroxide complexes, even at a pH as low as 2 (J, 2). To maintain iron in soluble form utilizable for the synthesis of essential iron-bearing enzymes and proteins, specific iron-binding molecules have evolved in many organisms.In the microbial world these iron-binders are relatively simple and well characterized structures, with hydroxamate or phenolate ligands at their active sites (3). Their function is to mobilize iron from its inorganic environment and to present it in soluble form to the organism. Further more they may be expendable; iron appears to be released from some of them for metabolic use by degradation of their molecular structure (4).In the vertebrate kingdom, where elaborate circulatory systems serve tissues with widely varying iron requirements, the transferrins, compris ing a more complex and more subtle class of iron-binding molecules, have evolved for the transport of iron. Serum transferrin is the prototype 104 Downloaded by UNIV OF MICHIGAN ANN ARBOR on February 18, 2015 |

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Pseudomonas aeruginosaand the general hospital: a six-year survey

Cited by 8 publications

References 13 publications

Microbial contamination of topical medicaments used in the treatment and prevention of pressure sores

Microbial contamination of topical medicaments used in the treatment and prevention of pressure sores

1H-NMR spectroscopic study on the binding of alcohols to soybean lipoxygenase-1

Transport of Iron by Transferrin

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