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Activity of human extravascular temocillin concentrations simulated in an in-vitro kinetic model against beta-lactamase producing gram-negative bacilli.

The Journal of antimicrobial chemotherapy

Cooper CE, White AR, Slocombe B.
PMID: 2050587
J Antimicrob Chemother. 1991 Jan;27(1):105-15. doi: 10.1093/jac/27.1.105.

An in-vitro kinetic model was used to demonstrate the bactericidal activity of concentrations of temocillin achieved in extravascular body fluids following a 1 g intravenous dosage in man. Concentrations of temocillin attainable in peripheral lymph were bactericidal for ampicillin-resistant...

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Cooper CE, White AR, Slocombe B. Activity of human extravascular temocillin concentrations simulated in an in-vitro kinetic model against beta-lactamase producing gram-negative bacilli. J Antimicrob Chemother. 1991;27(1):105-15doi: 10.1093/jac/27.1.105.
Cooper, C. E., White, A. R., & Slocombe, B. (1991). Activity of human extravascular temocillin concentrations simulated in an in-vitro kinetic model against beta-lactamase producing gram-negative bacilli. The Journal of antimicrobial chemotherapy, 27(1), 105-15. https://doi.org/10.1093/jac/27.1.105
Cooper, C E, et al. "Activity of human extravascular temocillin concentrations simulated in an in-vitro kinetic model against beta-lactamase producing gram-negative bacilli." The Journal of antimicrobial chemotherapy vol. 27,1 (1991): 105-15. doi: https://doi.org/10.1093/jac/27.1.105
Cooper CE, White AR, Slocombe B. Activity of human extravascular temocillin concentrations simulated in an in-vitro kinetic model against beta-lactamase producing gram-negative bacilli. J Antimicrob Chemother. 1991 Jan;27(1):105-15. doi: 10.1093/jac/27.1.105. PMID: 2050587.
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EPR differences between human myeloperoxidase isoenzymes.

Biochemical Society transactions

Cooper CE, Odell E.
PMID: 1327892
Biochem Soc Trans. 1992 May;20(2):108S. doi: 10.1042/bst020108s.

No abstract available.

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Cooper CE, Odell E. EPR differences between human myeloperoxidase isoenzymes. Biochem Soc Trans. 1992;20(2):108Sdoi: 10.1042/bst020108s.
Cooper, C. E., & Odell, E. (1992). EPR differences between human myeloperoxidase isoenzymes. Biochemical Society transactions, 20(2), 108S. https://doi.org/10.1042/bst020108s
Cooper, C E, and Odell, E. "EPR differences between human myeloperoxidase isoenzymes." Biochemical Society transactions vol. 20,2 (1992): 108S. doi: https://doi.org/10.1042/bst020108s
Cooper CE, Odell E. EPR differences between human myeloperoxidase isoenzymes. Biochem Soc Trans. 1992 May;20(2):108S. doi: 10.1042/bst020108s. PMID: 1327892.
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Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli.

The Biochemical journal

Ioannidis N, Cooper CE, Poole RK.
PMID: 1334413
Biochem J. 1992 Dec 01;288:649-55. doi: 10.1042/bj2880649.
Free PMC Article

The Escherichia coli haemoglobin-like flavohaemoprotein (Hmp) has been purified to near homogeneity using two chromatographic steps. The prosthetic groups are identified as FAD and protohaem IX. SDS/PAGE has indicated a molecular mass of 44 kDa for the monomeric protein...

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Ioannidis N, Cooper CE, Poole RK. Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. Biochem J. 1992;288:649-55doi: 10.1042/bj2880649.
Ioannidis, N., Cooper, C. E., & Poole, R. K. (1992). Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. The Biochemical journal, 288649-55. https://doi.org/10.1042/bj2880649
Ioannidis, N, et al. "Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli." The Biochemical journal vol. 288 (1992): 649-55. doi: https://doi.org/10.1042/bj2880649
Ioannidis N, Cooper CE, Poole RK. Spectroscopic studies on an oxygen-binding haemoglobin-like flavohaemoprotein from Escherichia coli. Biochem J. 1992 Dec 01;288:649-55. doi: 10.1042/bj2880649. PMID: 1334413; PMCID: PMC1132060.
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Non-transferrin-bound iron species in the serum of hypotransferrinaemic mice.

Biochimica et biophysica acta

Simpson RJ, Cooper CE, Raja KB, Halliwell B, Evans PJ, Aruoma OI, Singh S, Konijn AM.
PMID: 1335284
Biochim Biophys Acta. 1992 Dec 08;1156(1):19-26. doi: 10.1016/0304-4165(92)90090-h.

Serum from homozygous hypotransferrinaemic mice (a mixed group of males and females, aged 6-8 wk) was found to contain low levels of iron (mean 0.9 +/- 0.5 microM (SEM, n = 4), as assayed by conventional serum iron assays....

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Simpson RJ, Cooper CE, Raja KB, et al. Non-transferrin-bound iron species in the serum of hypotransferrinaemic mice. Biochim Biophys Acta. 1992;1156(1):19-26doi: 10.1016/0304-4165(92)90090-h.
Simpson, R. J., Cooper, C. E., Raja, K. B., Halliwell, B., Evans, P. J., Aruoma, O. I., Singh, S., & Konijn, A. M. (1992). Non-transferrin-bound iron species in the serum of hypotransferrinaemic mice. Biochimica et biophysica acta, 1156(1), 19-26. https://doi.org/10.1016/0304-4165(92)90090-h
Simpson, R J, et al. "Non-transferrin-bound iron species in the serum of hypotransferrinaemic mice." Biochimica et biophysica acta vol. 1156,1 (1992): 19-26. doi: https://doi.org/10.1016/0304-4165(92)90090-h
Simpson RJ, Cooper CE, Raja KB, Halliwell B, Evans PJ, Aruoma OI, Singh S, Konijn AM. Non-transferrin-bound iron species in the serum of hypotransferrinaemic mice. Biochim Biophys Acta. 1992 Dec 08;1156(1):19-26. doi: 10.1016/0304-4165(92)90090-h. PMID: 1335284.
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The proteoliposomal steady state. Effect of size, capacitance and membrane permeability on cytochrome-oxidase-induced ion gradients.

The Biochemical journal

Wrigglesworth JM, Cooper CE, Sharpe MA, Nicholls P.
PMID: 2168698
Biochem J. 1990 Aug 15;270(1):109-18. doi: 10.1042/bj2700109.
Free PMC Article

1. The flux pathways for H+ and K+ movements into and out of proteoliposomes incorporating cytochrome c oxidase have been investigated as a function of the electrical and geometrical properties of the vesicles. 2. The respiration-induced pH gradient (delta...

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Wrigglesworth JM, Cooper CE, Sharpe MA, et al. The proteoliposomal steady state. Effect of size, capacitance and membrane permeability on cytochrome-oxidase-induced ion gradients. Biochem J. 1990;270(1):109-18doi: 10.1042/bj2700109.
Wrigglesworth, J. M., Cooper, C. E., Sharpe, M. A., & Nicholls, P. (1990). The proteoliposomal steady state. Effect of size, capacitance and membrane permeability on cytochrome-oxidase-induced ion gradients. The Biochemical journal, 270(1), 109-18. https://doi.org/10.1042/bj2700109
Wrigglesworth, J M, et al. "The proteoliposomal steady state. Effect of size, capacitance and membrane permeability on cytochrome-oxidase-induced ion gradients." The Biochemical journal vol. 270,1 (1990): 109-18. doi: https://doi.org/10.1042/bj2700109
Wrigglesworth JM, Cooper CE, Sharpe MA, Nicholls P. The proteoliposomal steady state. Effect of size, capacitance and membrane permeability on cytochrome-oxidase-induced ion gradients. Biochem J. 1990 Aug 15;270(1):109-18. doi: 10.1042/bj2700109. PMID: 2168698; PMCID: PMC1131685.
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Transport of K+ and other cations across phospholipid membranes by nonesterified fatty acids.

The Journal of membrane biology

Sharpe MA, Cooper CE, Wrigglesworth JM.
PMID: 7966242
J Membr Biol. 1994 Jul;141(1):21-8. doi: 10.1007/BF00232870.

The rate of change of internal pH and transmembrane potential has been monitored in liposomes following the external addition of various cation salts. Oleic acid increases the transmembrane movement of H+ following the imposition of a K+ gradient. An...

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Sharpe MA, Cooper CE, Wrigglesworth JM. Transport of K+ and other cations across phospholipid membranes by nonesterified fatty acids. J Membr Biol. 1994;141(1):21-8doi: 10.1007/BF00232870.
Sharpe, M. A., Cooper, C. E., & Wrigglesworth, J. M. (1994). Transport of K+ and other cations across phospholipid membranes by nonesterified fatty acids. The Journal of membrane biology, 141(1), 21-8. https://doi.org/10.1007/BF00232870
Sharpe, M A, et al. "Transport of K+ and other cations across phospholipid membranes by nonesterified fatty acids." The Journal of membrane biology vol. 141,1 (1994): 21-8. doi: https://doi.org/10.1007/BF00232870
Sharpe MA, Cooper CE, Wrigglesworth JM. Transport of K+ and other cations across phospholipid membranes by nonesterified fatty acids. J Membr Biol. 1994 Jul;141(1):21-8. doi: 10.1007/BF00232870. PMID: 7966242.
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The steady-state kinetics of cytochrome c oxidation by cytochrome oxidase.

Biochimica et biophysica acta

Cooper CE.
PMID: 2164845
Biochim Biophys Acta. 1990 Jun 26;1017(3):187-203. doi: 10.1016/0005-2728(90)90184-6.

No abstract available.

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Cooper CE. The steady-state kinetics of cytochrome c oxidation by cytochrome oxidase. Biochim Biophys Acta. 1990;1017(3):187-203doi: 10.1016/0005-2728(90)90184-6.
Cooper, C. E. (1990). The steady-state kinetics of cytochrome c oxidation by cytochrome oxidase. Biochimica et biophysica acta, 1017(3), 187-203. https://doi.org/10.1016/0005-2728(90)90184-6
Cooper, C E. "The steady-state kinetics of cytochrome c oxidation by cytochrome oxidase." Biochimica et biophysica acta vol. 1017,3 (1990): 187-203. doi: https://doi.org/10.1016/0005-2728(90)90184-6
Cooper CE. The steady-state kinetics of cytochrome c oxidation by cytochrome oxidase. Biochim Biophys Acta. 1990 Jun 26;1017(3):187-203. doi: 10.1016/0005-2728(90)90184-6. PMID: 2164845.
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MRI measurements of cerebral deoxyhaemoglobin concentration [dHb]--correlation with near infrared spectroscopy (NIRS).

NMR in biomedicine

Punwani S, Ordidge RJ, Cooper CE, Amess P, Clemence M.
PMID: 9802470
NMR Biomed. 1998 Oct;11(6):281-9. doi: 10.1002/(sici)1099-1492(199810)11:6<281::aid-nbm529>3.0.co;2-6.

Changes in physiological parameters such as cerebral blood flow, cerebral blood volume, oxygen extraction, and the size and distribution of cerebral blood vessels, result in changes in the local concentration of deoxyhaemoglobin ([dHb]). The purpose of this study was...

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Punwani S, Ordidge RJ, Cooper CE, et al. MRI measurements of cerebral deoxyhaemoglobin concentration [dHb]--correlation with near infrared spectroscopy (NIRS). NMR Biomed. 1998;11(6):281-9doi: 10.1002/(sici)1099-1492(199810)11:6<281::aid-nbm529>3.0.co;2-6.
Punwani, S., Ordidge, R. J., Cooper, C. E., Amess, P., & Clemence, M. (1998). MRI measurements of cerebral deoxyhaemoglobin concentration [dHb]--correlation with near infrared spectroscopy (NIRS). NMR in biomedicine, 11(6), 281-9. https://doi.org/10.1002/(sici)1099-1492(199810)11:6<281::aid-nbm529>3.0.co;2-6
Punwani, S, et al. "MRI measurements of cerebral deoxyhaemoglobin concentration [dHb]--correlation with near infrared spectroscopy (NIRS)." NMR in biomedicine vol. 11,6 (1998): 281-9. doi: https://doi.org/10.1002/(sici)1099-1492(199810)11:6<281::aid-nbm529>3.0.co;2-6
Punwani S, Ordidge RJ, Cooper CE, Amess P, Clemence M. MRI measurements of cerebral deoxyhaemoglobin concentration [dHb]--correlation with near infrared spectroscopy (NIRS). NMR Biomed. 1998 Oct;11(6):281-9. doi: 10.1002/(sici)1099-1492(199810)11:6<281::aid-nbm529>3.0.co;2-6. PMID: 9802470.
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Reactions of cross-linked ferric haemoglobins with hydrogen peroxide.

Biochemical Society transactions

Dunne J, Svistunenko DA, Wilson MT, Alayash AI, Cooper CE.
PMID: 10047834
Biochem Soc Trans. 1998 Nov;26(4):S320. doi: 10.1042/bst026s320.

No abstract available.

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Dunne J, Svistunenko DA, Wilson MT, et al. Reactions of cross-linked ferric haemoglobins with hydrogen peroxide. Biochem Soc Trans. 1998;26(4):S320doi: 10.1042/bst026s320.
Dunne, J., Svistunenko, D. A., Wilson, M. T., Alayash, A. I., & Cooper, C. E. (1998). Reactions of cross-linked ferric haemoglobins with hydrogen peroxide. Biochemical Society transactions, 26(4), S320. https://doi.org/10.1042/bst026s320
Dunne, J, et al. "Reactions of cross-linked ferric haemoglobins with hydrogen peroxide." Biochemical Society transactions vol. 26,4 (1998): S320. doi: https://doi.org/10.1042/bst026s320
Dunne J, Svistunenko DA, Wilson MT, Alayash AI, Cooper CE. Reactions of cross-linked ferric haemoglobins with hydrogen peroxide. Biochem Soc Trans. 1998 Nov;26(4):S320. doi: 10.1042/bst026s320. PMID: 10047834.
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Nitric oxide as an effector and a substrate for cytochrome c oxidase.

Biochemical Society transactions

Nicholls P, Sharpe M, Torres J, Wilson MT, Cooper CE.
PMID: 10047837
Biochem Soc Trans. 1998 Nov;26(4):S323. doi: 10.1042/bst026s323.

No abstract available.

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Nicholls P, Sharpe M, Torres J, et al. Nitric oxide as an effector and a substrate for cytochrome c oxidase. Biochem Soc Trans. 1998;26(4):S323doi: 10.1042/bst026s323.
Nicholls, P., Sharpe, M., Torres, J., Wilson, M. T., & Cooper, C. E. (1998). Nitric oxide as an effector and a substrate for cytochrome c oxidase. Biochemical Society transactions, 26(4), S323. https://doi.org/10.1042/bst026s323
Nicholls, P, et al. "Nitric oxide as an effector and a substrate for cytochrome c oxidase." Biochemical Society transactions vol. 26,4 (1998): S323. doi: https://doi.org/10.1042/bst026s323
Nicholls P, Sharpe M, Torres J, Wilson MT, Cooper CE. Nitric oxide as an effector and a substrate for cytochrome c oxidase. Biochem Soc Trans. 1998 Nov;26(4):S323. doi: 10.1042/bst026s323. PMID: 10047837.
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The electron paramagnetic resonance characterisation of a copper-containing extracellular peroxidase from Thermomonospora fusca BD25.

Biochimica et biophysica acta

Svistunenko DA, Rob A, Ball A, Torres J, Symons MC, Wilson MT, Cooper CE.
PMID: 10556561
Biochim Biophys Acta. 1999 Sep 14;1434(1):74-85. doi: 10.1016/s0167-4838(99)00163-6.

The actinomycete Thermomonospora fusca BD25 contains a peroxidase with a high activity over a broad range of temperature and pH and a high stability against denaturing agents. Unusually this peroxidase (PO) is a non-haem enzyme. As prepared PO is...

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Svistunenko DA, Rob A, Ball A, et al. The electron paramagnetic resonance characterisation of a copper-containing extracellular peroxidase from Thermomonospora fusca BD25. Biochim Biophys Acta. 1999;1434(1):74-85doi: 10.1016/s0167-4838(99)00163-6.
Svistunenko, D. A., Rob, A., Ball, A., Torres, J., Symons, M. C., Wilson, M. T., & Cooper, C. E. (1999). The electron paramagnetic resonance characterisation of a copper-containing extracellular peroxidase from Thermomonospora fusca BD25. Biochimica et biophysica acta, 1434(1), 74-85. https://doi.org/10.1016/s0167-4838(99)00163-6
Svistunenko, D A, et al. "The electron paramagnetic resonance characterisation of a copper-containing extracellular peroxidase from Thermomonospora fusca BD25." Biochimica et biophysica acta vol. 1434,1 (1999): 74-85. doi: https://doi.org/10.1016/s0167-4838(99)00163-6
Svistunenko DA, Rob A, Ball A, Torres J, Symons MC, Wilson MT, Cooper CE. The electron paramagnetic resonance characterisation of a copper-containing extracellular peroxidase from Thermomonospora fusca BD25. Biochim Biophys Acta. 1999 Sep 14;1434(1):74-85. doi: 10.1016/s0167-4838(99)00163-6. PMID: 10556561.
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An automated system for the measurement of the response of cerebral blood volume and cerebral blood flow to changes in arterial carbon dioxide tension using near infrared spectroscopy.

Advances in experimental medicine and biology

Elwell CE, Cope M, Kirkby D, Owen-Reece H, Cooper CE, Reynolds EO, Delpy DT.
PMID: 7597937
Adv Exp Med Biol. 1994;361:143-55. doi: 10.1007/978-1-4615-1875-4_19.

No abstract available.

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Elwell CE, Cope M, Kirkby D, et al. An automated system for the measurement of the response of cerebral blood volume and cerebral blood flow to changes in arterial carbon dioxide tension using near infrared spectroscopy. Adv Exp Med Biol. 1994;361:143-55doi: 10.1007/978-1-4615-1875-4_19.
Elwell, C. E., Cope, M., Kirkby, D., Owen-Reece, H., Cooper, C. E., Reynolds, E. O., & Delpy, D. T. (1994). An automated system for the measurement of the response of cerebral blood volume and cerebral blood flow to changes in arterial carbon dioxide tension using near infrared spectroscopy. Advances in experimental medicine and biology, 361143-55. https://doi.org/10.1007/978-1-4615-1875-4_19
Elwell, C E, et al. "An automated system for the measurement of the response of cerebral blood volume and cerebral blood flow to changes in arterial carbon dioxide tension using near infrared spectroscopy." Advances in experimental medicine and biology vol. 361 (1994): 143-55. doi: https://doi.org/10.1007/978-1-4615-1875-4_19
Elwell CE, Cope M, Kirkby D, Owen-Reece H, Cooper CE, Reynolds EO, Delpy DT. An automated system for the measurement of the response of cerebral blood volume and cerebral blood flow to changes in arterial carbon dioxide tension using near infrared spectroscopy. Adv Exp Med Biol. 1994;361:143-55. doi: 10.1007/978-1-4615-1875-4_19. PMID: 7597937.
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Showing 1 to 12 of 274 entries