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The effects of azathioprine (imuran) on purine synthesis in clinical disorders of purine metabolism.

The Journal of clinical investigation

Kelley WN, Rosenbloom FM, Seegmiller JE.
PMID: 16695929
J Clin Invest. 1967 Sep;46(9):1518-29. doi: 10.1172/JCI105643.

Azathioprine, a purine analogue, significantly suppressed the purine synthesis de novo of two gouty patients manifesting overproduction of uric acid, as well as three of four gouty patients who showed normal uric acid production. This suppression is taken as...

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Kelley WN, Rosenbloom FM, Seegmiller JE. The effects of azathioprine (imuran) on purine synthesis in clinical disorders of purine metabolism. J Clin Invest. 1967;46(9):1518-29doi: 10.1172/JCI105643.
Kelley, W. N., Rosenbloom, F. M., & Seegmiller, J. E. (1967). The effects of azathioprine (imuran) on purine synthesis in clinical disorders of purine metabolism. The Journal of clinical investigation, 46(9), 1518-29. https://doi.org/10.1172/JCI105643
Kelley, W N, et al. "The effects of azathioprine (imuran) on purine synthesis in clinical disorders of purine metabolism." The Journal of clinical investigation vol. 46,9 (1967): 1518-29. doi: https://doi.org/10.1172/JCI105643
Kelley WN, Rosenbloom FM, Seegmiller JE. The effects of azathioprine (imuran) on purine synthesis in clinical disorders of purine metabolism. J Clin Invest. 1967 Sep;46(9):1518-29. doi: 10.1172/JCI105643. PMID: 16695929; PMCID: PMC292897.
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Superoxide free radicals are produced in glyoxysomes.

Plant physiology

Sandalio LM, Fernández VM, Rupérez FL, Del Río LA.
PMID: 16666081
Plant Physiol. 1988 May;87(1):1-4. doi: 10.1104/pp.87.1.1.

The production of superoxide free radicals in pellet and supernatant fractions of glyoxysomes, specialized plant peroxisomes from watermelon (Citrullus vulgaris Schrad.) cotyledons, was investigated. Upon inhibition of the endogenous superoxide dismutase, xanthine, and hypoxanthine induced in glyoxysomal supernatants the...

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Sandalio LM, Fernández VM, Rupérez FL, et al. Superoxide free radicals are produced in glyoxysomes. Plant Physiol. 1988;87(1):1-4doi: 10.1104/pp.87.1.1.
Sandalio, L. M., Fernández, V. M., Rupérez, F. L., & Del Río, L. A. (1988). Superoxide free radicals are produced in glyoxysomes. Plant physiology, 87(1), 1-4. https://doi.org/10.1104/pp.87.1.1
Sandalio, L M, et al. "Superoxide free radicals are produced in glyoxysomes." Plant physiology vol. 87,1 (1988): 1-4. doi: https://doi.org/10.1104/pp.87.1.1
Sandalio LM, Fernández VM, Rupérez FL, Del Río LA. Superoxide free radicals are produced in glyoxysomes. Plant Physiol. 1988 May;87(1):1-4. doi: 10.1104/pp.87.1.1. PMID: 16666081; PMCID: PMC1054687.
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Purine catabolism in plants : purification and some properties of inosine nucleosidase from yellow lupin (lupinus luteus L.) seeds.

Plant physiology

Guranowski A.
PMID: 16662492
Plant Physiol. 1982 Aug;70(2):344-9. doi: 10.1104/pp.70.2.344.

Inosine nucleosidase (EC 3.2.2.2), the enzyme which hydrolyzes inosine to hypoxanthine and ribose, has been partially purified from Lupinus luteus L. cv. Topaz seeds by extraction of the seed meal with low ionic strength buffer, ammonium sulfate fractionation, and...

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Guranowski A. Purine catabolism in plants : purification and some properties of inosine nucleosidase from yellow lupin (lupinus luteus L.) seeds. Plant Physiol. 1982;70(2):344-9doi: 10.1104/pp.70.2.344.
Guranowski, A. (1982). Purine catabolism in plants : purification and some properties of inosine nucleosidase from yellow lupin (lupinus luteus L.) seeds. Plant physiology, 70(2), 344-9. https://doi.org/10.1104/pp.70.2.344
Guranowski, A. "Purine catabolism in plants : purification and some properties of inosine nucleosidase from yellow lupin (lupinus luteus L.) seeds." Plant physiology vol. 70,2 (1982): 344-9. doi: https://doi.org/10.1104/pp.70.2.344
Guranowski A. Purine catabolism in plants : purification and some properties of inosine nucleosidase from yellow lupin (lupinus luteus L.) seeds. Plant Physiol. 1982 Aug;70(2):344-9. doi: 10.1104/pp.70.2.344. PMID: 16662492; PMCID: PMC1067146.
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Purine-phosphoribosyltransferase activities in rat and mouse tissues and in Ehrlich ascites-tumour cells.

The Biochemical journal

Murray AW.
PMID: 16742414
Biochem J. 1966 Sep;100(3):664-70. doi: 10.1042/bj1000664.

1. The activities of adenine phosphoribosyltransferase and hypoxanthine phosphoribosyltransferase in extracts of rat and mouse liver, brain, spleen, heart and kidney, of rat bone marrow and of Ehrlich ascites-tumour cells have been measured. The specific activity of adenine phosphoribosyltransferase...

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Murray AW. Purine-phosphoribosyltransferase activities in rat and mouse tissues and in Ehrlich ascites-tumour cells. Biochem J. 1966;100(3):664-70doi: 10.1042/bj1000664.
Murray, A. W. (1966). Purine-phosphoribosyltransferase activities in rat and mouse tissues and in Ehrlich ascites-tumour cells. The Biochemical journal, 100(3), 664-70. https://doi.org/10.1042/bj1000664
Murray, A W. "Purine-phosphoribosyltransferase activities in rat and mouse tissues and in Ehrlich ascites-tumour cells." The Biochemical journal vol. 100,3 (1966): 664-70. doi: https://doi.org/10.1042/bj1000664
Murray AW. Purine-phosphoribosyltransferase activities in rat and mouse tissues and in Ehrlich ascites-tumour cells. Biochem J. 1966 Sep;100(3):664-70. doi: 10.1042/bj1000664. PMID: 16742414; PMCID: PMC1265199.
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Enzyme sensors for determination of fish freshness.

Talanta

Volpe G, Mascini M.
PMID: 18966489
Talanta. 1996 Feb;43(2):283-9. doi: 10.1016/0039-9140(95)01758-5.

A simple and rapid procedure for the determination of fish freshness was developed and applied to the determination of the K(1) parameter (freshness indicator): K(1) = ([HXR] + [HX])/([IMP] + [HXR] + [HX]) x 100, where [IMP], [HXR] and...

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Volpe G, Mascini M. Enzyme sensors for determination of fish freshness. Talanta. 1996;43(2):283-9doi: 10.1016/0039-9140(95)01758-5.
Volpe, G., & Mascini, M. (1996). Enzyme sensors for determination of fish freshness. Talanta, 43(2), 283-9. https://doi.org/10.1016/0039-9140(95)01758-5
Volpe, G, and Mascini, M. "Enzyme sensors for determination of fish freshness." Talanta vol. 43,2 (1996): 283-9. doi: https://doi.org/10.1016/0039-9140(95)01758-5
Volpe G, Mascini M. Enzyme sensors for determination of fish freshness. Talanta. 1996 Feb;43(2):283-9. doi: 10.1016/0039-9140(95)01758-5. PMID: 18966489.
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Amperometric detection of uric acid and hypoxanthine with Xanthine oxidase immobilized and carbon based screen-printed electrode. Application for fish freshness determination.

Talanta

Carsol MA, Volpe G, Mascini M.
PMID: 18966965
Talanta. 1997 Nov;44(11):2151-9. doi: 10.1016/s0039-9140(97)00098-2.

Carbon-based screen-printed electrodes are suitable for uric acid detection. Xanthine oxidase (XO) was immobilized either directly on the surface of the electrode or in a reactor with CPG aminopropylsilane in a FIA assembly. Higher reproducibility and lifetime was obtained...

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Carsol MA, Volpe G, Mascini M. Amperometric detection of uric acid and hypoxanthine with Xanthine oxidase immobilized and carbon based screen-printed electrode. Application for fish freshness determination. Talanta. 1997;44(11):2151-9doi: 10.1016/s0039-9140(97)00098-2.
Carsol, M. A., Volpe, G., & Mascini, M. (1997). Amperometric detection of uric acid and hypoxanthine with Xanthine oxidase immobilized and carbon based screen-printed electrode. Application for fish freshness determination. Talanta, 44(11), 2151-9. https://doi.org/10.1016/s0039-9140(97)00098-2
Carsol, M A, et al. "Amperometric detection of uric acid and hypoxanthine with Xanthine oxidase immobilized and carbon based screen-printed electrode. Application for fish freshness determination." Talanta vol. 44,11 (1997): 2151-9. doi: https://doi.org/10.1016/s0039-9140(97)00098-2
Carsol MA, Volpe G, Mascini M. Amperometric detection of uric acid and hypoxanthine with Xanthine oxidase immobilized and carbon based screen-printed electrode. Application for fish freshness determination. Talanta. 1997 Nov;44(11):2151-9. doi: 10.1016/s0039-9140(97)00098-2. PMID: 18966965.
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Chemical, sensory and shelf life evaluation of sliced salmon treated with salts of organic acids.

Food chemistry

Sallam KI.
PMID: 17245440
Food Chem. 2007;101(2):592-600. doi: 10.1016/j.foodchem.2006.02.019.

This study was carried out to evaluate the shelf life, chemical quality and sensory attributes of salmon slices treated by dipping in 2.5% aqueous solution of sodium acetate (NaA), sodium lactate (NaL), or sodium citrate (NaC) during refrigerated storage...

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Sallam KI. Chemical, sensory and shelf life evaluation of sliced salmon treated with salts of organic acids. Food Chem. 2007;101(2):592-600doi: 10.1016/j.foodchem.2006.02.019.
Sallam, K. I. (2007). Chemical, sensory and shelf life evaluation of sliced salmon treated with salts of organic acids. Food chemistry, 101(2), 592-600. https://doi.org/10.1016/j.foodchem.2006.02.019
Sallam, Khalid Ibrahim. "Chemical, sensory and shelf life evaluation of sliced salmon treated with salts of organic acids." Food chemistry vol. 101,2 (2007): 592-600. doi: https://doi.org/10.1016/j.foodchem.2006.02.019
Sallam KI. Chemical, sensory and shelf life evaluation of sliced salmon treated with salts of organic acids. Food Chem. 2007;101(2):592-600. doi: 10.1016/j.foodchem.2006.02.019. PMID: 17245440; PMCID: PMC1780258.
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WITHDRAWN:Chimeric hypoxanthine guanine phosphoribosyltransferases: Effect of segment swapping on xanthine specificity and tetramer stability.

The Biochemical journal

Ashok CS, Subbayya SI, Selvi ST, Balaram H.
PMID: 16716144
Biochem J. 2006 May 22; doi: 10.1042/BJ20060113. Epub 2006 May 22.

The paper entitled "Chimeric hypoxanthine guanine phosphoribosyltransferases: Effect of segment on xanthine specificity and tetramer stability", which was published online on 22 May 2006, was withdrawn at the author's request.

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Ashok CS, Subbayya SI, Selvi ST, et al. WITHDRAWN:Chimeric hypoxanthine guanine phosphoribosyltransferases: Effect of segment swapping on xanthine specificity and tetramer stability. Biochem J. 2006;doi: 10.1042/BJ20060113.
Ashok, C. S., Subbayya, S. I., Selvi, S. T., & Balaram, H. (2006). WITHDRAWN:Chimeric hypoxanthine guanine phosphoribosyltransferases: Effect of segment swapping on xanthine specificity and tetramer stability. The Biochemical journal, . https://doi.org/10.1042/BJ20060113
Ashok, Chethan S, et al. "WITHDRAWN:Chimeric hypoxanthine guanine phosphoribosyltransferases: Effect of segment swapping on xanthine specificity and tetramer stability." The Biochemical journal vol. (2006). doi: https://doi.org/10.1042/BJ20060113
Ashok CS, Subbayya SI, Selvi ST, Balaram H. WITHDRAWN:Chimeric hypoxanthine guanine phosphoribosyltransferases: Effect of segment swapping on xanthine specificity and tetramer stability. Biochem J. 2006 May 22; doi: 10.1042/BJ20060113. Epub 2006 May 22. PMID: 16716144.
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Retention of enzyme by electropolymerized film: a new approach in developing a hypoxanthine biosensor.

Biotechnology and bioengineering

Nguyen AL, Luong JH, Yacynych AM.
PMID: 18600669
Biotechnol Bioeng. 1991 Apr 05;37(8):729-35. doi: 10.1002/bit.260370807.

An amperometric biosensor for hypoxanthine was constructed by forming a layer of crosslinked xanthine oxidase on a platinum electrode, followed by electropolymerization of a submonolayer film of resorcinol and para-diaminobenzene. The fabricated electrodes were evaluated for speed of response,...

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Nguyen AL, Luong JH, Yacynych AM. Retention of enzyme by electropolymerized film: a new approach in developing a hypoxanthine biosensor. Biotechnol Bioeng. 1991;37(8):729-35doi: 10.1002/bit.260370807.
Nguyen, A. L., Luong, J. H., & Yacynych, A. M. (1991). Retention of enzyme by electropolymerized film: a new approach in developing a hypoxanthine biosensor. Biotechnology and bioengineering, 37(8), 729-35. https://doi.org/10.1002/bit.260370807
Nguyen, A L, et al. "Retention of enzyme by electropolymerized film: a new approach in developing a hypoxanthine biosensor." Biotechnology and bioengineering vol. 37,8 (1991): 729-35. doi: https://doi.org/10.1002/bit.260370807
Nguyen AL, Luong JH, Yacynych AM. Retention of enzyme by electropolymerized film: a new approach in developing a hypoxanthine biosensor. Biotechnol Bioeng. 1991 Apr 05;37(8):729-35. doi: 10.1002/bit.260370807. PMID: 18600669.
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Antimalarial activity of fractions isolated from Albizia gummifera and Aspilia mossambicensis crude extracts.

African journal of health sciences

Orulla AV, Rukunga GM, Chege GM, Kiarie F, Muthaura CN, Githure JI, Kofi-Tsekpo WM.
PMID: 17451297
Afr J Health Sci. 1996 May;3(2):44-6.

To identify the fractions of medicinal plant extracts containing the highest concentration of antimalarial principles, we tested the antimalarial activities of the crude or total extracts and two fractions from Albizia gummifera (Leguminosae) and three fractions from Aspilia mossambicencis...

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Orulla AV, Rukunga GM, Chege GM, et al. Antimalarial activity of fractions isolated from Albizia gummifera and Aspilia mossambicensis crude extracts. Afr J Health Sci. 1996;3(2):44-6
Orulla, A. V., Rukunga, G. M., Chege, G. M., Kiarie, F., Muthaura, C. N., Githure, J. I., & Kofi-Tsekpo, W. M. (1996). Antimalarial activity of fractions isolated from Albizia gummifera and Aspilia mossambicensis crude extracts. African journal of health sciences, 3(2), 44-6.
Orulla, A V, et al. "Antimalarial activity of fractions isolated from Albizia gummifera and Aspilia mossambicensis crude extracts." African journal of health sciences vol. 3,2 (1996): 44-6.
Orulla AV, Rukunga GM, Chege GM, Kiarie F, Muthaura CN, Githure JI, Kofi-Tsekpo WM. Antimalarial activity of fractions isolated from Albizia gummifera and Aspilia mossambicensis crude extracts. Afr J Health Sci. 1996 May;3(2):44-6. PMID: 17451297.
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Application of a universal solvation model to nucleic acid bases: comparison of semiempirical molecular orbital theory, ab initio Hartree-Fock theory, and density functional theory.

Biophysical chemistry

Li J, Cramer CJ, Truhlar DG.
PMID: 17030308
Biophys Chem. 1999 Apr 05;78(1):147-55. doi: 10.1016/s0301-4622(98)00228-2.

The free energies of solvation of six nucleic acid bases (adenine, cytosine, hypoxanthine, guanine, thymine, and uracil) in water and chloroform are calculated using CM2 class IV charges and SM5.42R atomic surface tensions. Using any of three approximations to...

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Li J, Cramer CJ, Truhlar DG. Application of a universal solvation model to nucleic acid bases: comparison of semiempirical molecular orbital theory, ab initio Hartree-Fock theory, and density functional theory. Biophys Chem. 1999;78(1):147-55doi: 10.1016/s0301-4622(98)00228-2.
Li, J., Cramer, C. J., & Truhlar, D. G. (1999). Application of a universal solvation model to nucleic acid bases: comparison of semiempirical molecular orbital theory, ab initio Hartree-Fock theory, and density functional theory. Biophysical chemistry, 78(1), 147-55. https://doi.org/10.1016/s0301-4622(98)00228-2
Li, J, et al. "Application of a universal solvation model to nucleic acid bases: comparison of semiempirical molecular orbital theory, ab initio Hartree-Fock theory, and density functional theory." Biophysical chemistry vol. 78,1 (1999): 147-55. doi: https://doi.org/10.1016/s0301-4622(98)00228-2
Li J, Cramer CJ, Truhlar DG. Application of a universal solvation model to nucleic acid bases: comparison of semiempirical molecular orbital theory, ab initio Hartree-Fock theory, and density functional theory. Biophys Chem. 1999 Apr 05;78(1):147-55. doi: 10.1016/s0301-4622(98)00228-2. PMID: 17030308.
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Potent radical-scavenging activities of thiamin and thiamin diphosphate.

Journal of clinical biochemistry and nutrition

Okai Y, Higashi-Okai K, F Sato E, Konaka R, Inoue M.
PMID: 18437212
J Clin Biochem Nutr. 2007 Jan;40(1):42-8. doi: 10.3164/jcbn.40.42.

Various radical-scavenging activities of thiamin and thiamin diphosphate (TDP) were found in some in vitro experiments. Thiamin and TDP caused considerable suppressive effects on superoxide generation in hypoxanthine and xanthine oxidase system which was measured by a sensitive chemiluminescence...

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Okai Y, Higashi-Okai K, F Sato E, et al. Potent radical-scavenging activities of thiamin and thiamin diphosphate. J Clin Biochem Nutr. 2007;40(1):42-8doi: 10.3164/jcbn.40.42.
Okai, Y., Higashi-Okai, K., F Sato, E., Konaka, R., & Inoue, M. (2007). Potent radical-scavenging activities of thiamin and thiamin diphosphate. Journal of clinical biochemistry and nutrition, 40(1), 42-8. https://doi.org/10.3164/jcbn.40.42
Okai, Yasuji, et al. "Potent radical-scavenging activities of thiamin and thiamin diphosphate." Journal of clinical biochemistry and nutrition vol. 40,1 (2007): 42-8. doi: https://doi.org/10.3164/jcbn.40.42
Okai Y, Higashi-Okai K, F Sato E, Konaka R, Inoue M. Potent radical-scavenging activities of thiamin and thiamin diphosphate. J Clin Biochem Nutr. 2007 Jan;40(1):42-8. doi: 10.3164/jcbn.40.42. PMID: 18437212; PMCID: PMC2291503.
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Showing 13 to 24 of 449 entries