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Immunochemical studies on xanthine dehydrogenase of soybean root nodules : Ontogenic changes in the level of enzyme and immunocytochemical localization.

Planta

Nguyen J, Machal L, Vidal J, Perrot-Rechenmann C, Gadal P.
PMID: 24241850
Planta. 1986 Feb;167(2):190-5. doi: 10.1007/BF00391414.

Xanthine dehydrogenase (XDH, EC 1.2.1.37) was purified from root nodules of soybean (Glycine max) and used to prepare a polyclonal rabbit antiserum. Monospecificity of this antiserum was ascertained by sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the immunoprecipate. During root...

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Nguyen J, Machal L, Vidal J, et al. Immunochemical studies on xanthine dehydrogenase of soybean root nodules : Ontogenic changes in the level of enzyme and immunocytochemical localization. Planta. 1986;167(2):190-5doi: 10.1007/BF00391414.
Nguyen, J., Machal, L., Vidal, J., Perrot-Rechenmann, C., & Gadal, P. (1986). Immunochemical studies on xanthine dehydrogenase of soybean root nodules : Ontogenic changes in the level of enzyme and immunocytochemical localization. Planta, 167(2), 190-5. https://doi.org/10.1007/BF00391414
Nguyen, J, et al. "Immunochemical studies on xanthine dehydrogenase of soybean root nodules : Ontogenic changes in the level of enzyme and immunocytochemical localization." Planta vol. 167,2 (1986): 190-5. doi: https://doi.org/10.1007/BF00391414
Nguyen J, Machal L, Vidal J, Perrot-Rechenmann C, Gadal P. Immunochemical studies on xanthine dehydrogenase of soybean root nodules : Ontogenic changes in the level of enzyme and immunocytochemical localization. Planta. 1986 Feb;167(2):190-5. doi: 10.1007/BF00391414. PMID: 24241850.
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Linking uric acid metabolism to diabetic complications.

World journal of diabetes

Kushiyama A, Tanaka K, Hara S, Kawazu S.
PMID: 25512781
World J Diabetes. 2014 Dec 15;5(6):787-95. doi: 10.4239/wjd.v5.i6.787.

Hyperuricemia have been thought to be caused by the ingestion of large amounts of purines, and prevention or treatment of hyperuricemia has intended to prevent gout. Xanthine dehydrogenase/xanthine oxidase (XDH/XO) is rate-limiting enzyme of uric acid generation, and allopurinol...

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Kushiyama A, Tanaka K, Hara S, et al. Linking uric acid metabolism to diabetic complications. World J Diabetes. 2014;5(6):787-95doi: 10.4239/wjd.v5.i6.787.
Kushiyama, A., Tanaka, K., Hara, S., & Kawazu, S. (2014). Linking uric acid metabolism to diabetic complications. World journal of diabetes, 5(6), 787-95. https://doi.org/10.4239/wjd.v5.i6.787
Kushiyama, Akifumi, et al. "Linking uric acid metabolism to diabetic complications." World journal of diabetes vol. 5,6 (2014): 787-95. doi: https://doi.org/10.4239/wjd.v5.i6.787
Kushiyama A, Tanaka K, Hara S, Kawazu S. Linking uric acid metabolism to diabetic complications. World J Diabetes. 2014 Dec 15;5(6):787-95. doi: 10.4239/wjd.v5.i6.787. PMID: 25512781; PMCID: PMC4265865.
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Regeneration of fully nitrate reductase - deficient mutants from protoplast culture of Nicotiana plumbaginifolia (Viviani).

TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik

Negrutiu I, Dirks R, Jacobs M.
PMID: 24263936
Theor Appl Genet. 1983 Sep;66(3):341-7. doi: 10.1007/BF00251169.

Protoplast-derived colonies of haploid N. plumbaginifolia were selected for by chlorate resistance in media supplemented with casamino acids. Eighty resistant lines were confirmed by a second passage on a higher concentration of chlorate. Frequency of spontaneous mutation ranged from...

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Negrutiu I, Dirks R, Jacobs M. Regeneration of fully nitrate reductase - deficient mutants from protoplast culture of Nicotiana plumbaginifolia (Viviani). Theor Appl Genet. 1983;66(3):341-7doi: 10.1007/BF00251169.
Negrutiu, I., Dirks, R., & Jacobs, M. (1983). Regeneration of fully nitrate reductase - deficient mutants from protoplast culture of Nicotiana plumbaginifolia (Viviani). TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik, 66(3), 341-7. https://doi.org/10.1007/BF00251169
Negrutiu, I, et al. "Regeneration of fully nitrate reductase - deficient mutants from protoplast culture of Nicotiana plumbaginifolia (Viviani)." TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik vol. 66,3 (1983): 341-7. doi: https://doi.org/10.1007/BF00251169
Negrutiu I, Dirks R, Jacobs M. Regeneration of fully nitrate reductase - deficient mutants from protoplast culture of Nicotiana plumbaginifolia (Viviani). Theor Appl Genet. 1983 Sep;66(3):341-7. doi: 10.1007/BF00251169. PMID: 24263936.
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Crosstalk of Various Biomarkers That Might Provide Prompt Identification of Acute or Chronic Cardiorenal Syndromes.

Cardiorenal medicine

Tasić D, Radenkovic S, Stojanovic D, Milojkovic M, Stojanovic M, Ilic MD, Kocic G.
PMID: 26989395
Cardiorenal Med. 2016 Feb;6(2):99-107. doi: 10.1159/000437309. Epub 2015 Nov 11.

INTRODUCTION: Pathophysiological interaction between the heart and kidneys represents the basis for clinical entities called cardiorenal syndromes. The purpose of the study was to assess the relations between acute and chronic cardiorenal syndromes and biomarkers [advanced oxidation protein products,...

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Tasić D, Radenkovic S, Stojanovic D, et al. Crosstalk of Various Biomarkers That Might Provide Prompt Identification of Acute or Chronic Cardiorenal Syndromes. Cardiorenal Med. 2015;6(2):99-107doi: 10.1159/000437309.
Tasić, D., Radenkovic, S., Stojanovic, D., Milojkovic, M., Stojanovic, M., Ilic, M. D., & Kocic, G. (2016). Crosstalk of Various Biomarkers That Might Provide Prompt Identification of Acute or Chronic Cardiorenal Syndromes. Cardiorenal medicine, 6(2), 99-107. https://doi.org/10.1159/000437309
Tasić, Danijela, et al. "Crosstalk of Various Biomarkers That Might Provide Prompt Identification of Acute or Chronic Cardiorenal Syndromes." Cardiorenal medicine vol. 6,2 (2016): 99-107. doi: https://doi.org/10.1159/000437309
Tasić D, Radenkovic S, Stojanovic D, Milojkovic M, Stojanovic M, Ilic MD, Kocic G. Crosstalk of Various Biomarkers That Might Provide Prompt Identification of Acute or Chronic Cardiorenal Syndromes. Cardiorenal Med. 2016 Feb;6(2):99-107. doi: 10.1159/000437309. Epub 2015 Nov 11. PMID: 26989395; PMCID: PMC4789923.
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Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation.

Proceedings of the National Academy of Sciences of the United States of America

Potrikus CJ, Breznak JA.
PMID: 16593064
Proc Natl Acad Sci U S A. 1981 Jul;78(7):4601-5. doi: 10.1073/pnas.78.7.4601.

Reticulitermes flavipes termites synthesize uric acid via purine-nucleoside phosphorylase (purine-nucleoside: orthophosphate ribosyltransferase, EC 2.4.2.1) and xanthine dehydrogenase (xanthine:NAD(+) oxidoreductase, EC 1.2.1.37), but their tissues lack uricase (urate:oxygen oxidoreductase, EC 1.7.3.3) or any other enzyme that degrades uric acid. Nevertheless,...

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Potrikus CJ, Breznak JA. Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation. Proc Natl Acad Sci U S A. 1981;78(7):4601-5doi: 10.1073/pnas.78.7.4601.
Potrikus, C. J., & Breznak, J. A. (1981). Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation. Proceedings of the National Academy of Sciences of the United States of America, 78(7), 4601-5. https://doi.org/10.1073/pnas.78.7.4601
Potrikus, C J, and Breznak, J A. "Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation." Proceedings of the National Academy of Sciences of the United States of America vol. 78,7 (1981): 4601-5. doi: https://doi.org/10.1073/pnas.78.7.4601
Potrikus CJ, Breznak JA. Gut bacteria recycle uric acid nitrogen in termites: A strategy for nutrient conservation. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4601-5. doi: 10.1073/pnas.78.7.4601. PMID: 16593064; PMCID: PMC319841.
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Enzymes of amide and ureide biogenesis in developing soybean nodules.

Plant physiology

Reynolds PH, Boland MJ, Blevins DG, Schubert KR, Randall DD.
PMID: 16662397
Plant Physiol. 1982 Jun;69(6):1334-8. doi: 10.1104/pp.69.6.1334.

Amide and ureide biogenic enzymes were measured in the plant fraction of soybean (Glycine max) nodules during the period 11 to 23 days after inoculation with Rhizobium japonicum (USDA 3I1b142). Enzymes involved in the initial assimilation of ammonia, i.e....

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Reynolds PH, Boland MJ, Blevins DG, et al. Enzymes of amide and ureide biogenesis in developing soybean nodules. Plant Physiol. 1982;69(6):1334-8doi: 10.1104/pp.69.6.1334.
Reynolds, P. H., Boland, M. J., Blevins, D. G., Schubert, K. R., & Randall, D. D. (1982). Enzymes of amide and ureide biogenesis in developing soybean nodules. Plant physiology, 69(6), 1334-8. https://doi.org/10.1104/pp.69.6.1334
Reynolds, P H, et al. "Enzymes of amide and ureide biogenesis in developing soybean nodules." Plant physiology vol. 69,6 (1982): 1334-8. doi: https://doi.org/10.1104/pp.69.6.1334
Reynolds PH, Boland MJ, Blevins DG, Schubert KR, Randall DD. Enzymes of amide and ureide biogenesis in developing soybean nodules. Plant Physiol. 1982 Jun;69(6):1334-8. doi: 10.1104/pp.69.6.1334. PMID: 16662397; PMCID: PMC426412.
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Allelic Variants at the Xanthine Dehydrogenase Locus Affecting Enzyme Activity in DROSOPHILA PSEUDOOBSCURA.

Genetics

Prakash S.
PMID: 17248755
Genetics. 1977 Sep;87(1):159-68. doi: 10.1093/genetics/87.1.159.

Quantitative studies of enzyme activity on gels show about four-fold differences in enzyme activity of different xanthine dehydrogenase (XDH ) alleles. At least three different activity classes could be distinguished among the 23 strains isogenic for the XDH locus....

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Prakash S. Allelic Variants at the Xanthine Dehydrogenase Locus Affecting Enzyme Activity in DROSOPHILA PSEUDOOBSCURA. Genetics. 1977;87(1):159-68doi: 10.1093/genetics/87.1.159.
Prakash, S. (1977). Allelic Variants at the Xanthine Dehydrogenase Locus Affecting Enzyme Activity in DROSOPHILA PSEUDOOBSCURA. Genetics, 87(1), 159-68. https://doi.org/10.1093/genetics/87.1.159
Prakash, S. "Allelic Variants at the Xanthine Dehydrogenase Locus Affecting Enzyme Activity in DROSOPHILA PSEUDOOBSCURA." Genetics vol. 87,1 (1977): 159-68. doi: https://doi.org/10.1093/genetics/87.1.159
Prakash S. Allelic Variants at the Xanthine Dehydrogenase Locus Affecting Enzyme Activity in DROSOPHILA PSEUDOOBSCURA. Genetics. 1977 Sep;87(1):159-68. doi: 10.1093/genetics/87.1.159. PMID: 17248755; PMCID: PMC1213723.
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Intercellular nodule localization and nodule specificity of xanthine dehydrogenase in soybean.

Plant physiology

Triplett EW.
PMID: 16664136
Plant Physiol. 1985 Apr;77(4):1004-9. doi: 10.1104/pp.77.4.1004.

The distribution of xanthine dehydrogenase throughout the soybean plant as well as the intercellular localization of xanthine dehydrogenase within soybean nodules was determined. Polyclonal antibodies against purified xanthine dehydrogenase were prepared and used in an enzymelinked immunosorbent assay to...

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Triplett EW. Intercellular nodule localization and nodule specificity of xanthine dehydrogenase in soybean. Plant Physiol. 1985;77(4):1004-9doi: 10.1104/pp.77.4.1004.
Triplett, E. W. (1985). Intercellular nodule localization and nodule specificity of xanthine dehydrogenase in soybean. Plant physiology, 77(4), 1004-9. https://doi.org/10.1104/pp.77.4.1004
Triplett, E W. "Intercellular nodule localization and nodule specificity of xanthine dehydrogenase in soybean." Plant physiology vol. 77,4 (1985): 1004-9. doi: https://doi.org/10.1104/pp.77.4.1004
Triplett EW. Intercellular nodule localization and nodule specificity of xanthine dehydrogenase in soybean. Plant Physiol. 1985 Apr;77(4):1004-9. doi: 10.1104/pp.77.4.1004. PMID: 16664136; PMCID: PMC1064648.
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Uricase and allantoinase in glyoxysomes.

Plant physiology

Theimer RR, Beevers H.
PMID: 16657604
Plant Physiol. 1971 Feb;47(2):246-51. doi: 10.1104/pp.47.2.246.

In fat-degrading tissues of seedlings of seven different plant species examined, uricase activity (urate:O(2) oxidoreductase, EC 1.7.33) was associated with particulate fractions. After equilibrium density centrifugation on sucrose density gradients the enzyme activity was recovered in the glyoxysomal band...

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Theimer RR, Beevers H. Uricase and allantoinase in glyoxysomes. Plant Physiol. 1971;47(2):246-51doi: 10.1104/pp.47.2.246.
Theimer, R. R., & Beevers, H. (1971). Uricase and allantoinase in glyoxysomes. Plant physiology, 47(2), 246-51. https://doi.org/10.1104/pp.47.2.246
Theimer, R R, and Beevers, H. "Uricase and allantoinase in glyoxysomes." Plant physiology vol. 47,2 (1971): 246-51. doi: https://doi.org/10.1104/pp.47.2.246
Theimer RR, Beevers H. Uricase and allantoinase in glyoxysomes. Plant Physiol. 1971 Feb;47(2):246-51. doi: 10.1104/pp.47.2.246. PMID: 16657604; PMCID: PMC365850.
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Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila.

Journal of the American Aging Association

Kim YS, Nam HJ, Chung HY, Kim ND, Ryu JH, Lee WJ, Arking R, Yoo MA.
PMID: 23604884
J Am Aging Assoc. 2001 Oct;24(4):187-93. doi: 10.1007/s11357-001-0020-6.

It has been proposed that uric acid is an important scavenger of deleterious oxygen species and peroxynitrite in biological systems. The cellular sources responsible for the generation of damage-causing reactive oxygen species (ROS) are widespread. Xanthine dehydrogenase (XDH) /...

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Kim YS, Nam HJ, Chung HY, et al. Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila. J Am Aging Assoc. 2001;24(4):187-93doi: 10.1007/s11357-001-0020-6.
Kim, Y. S., Nam, H. J., Chung, H. Y., Kim, N. D., Ryu, J. H., Lee, W. J., Arking, R., & Yoo, M. A. (2001). Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila. Journal of the American Aging Association, 24(4), 187-93. https://doi.org/10.1007/s11357-001-0020-6
Kim, Y S, et al. "Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila." Journal of the American Aging Association vol. 24,4 (2001): 187-93. doi: https://doi.org/10.1007/s11357-001-0020-6
Kim YS, Nam HJ, Chung HY, Kim ND, Ryu JH, Lee WJ, Arking R, Yoo MA. Role of xanthine dehydrogenase and aging on the innate immune response of Drosophila. J Am Aging Assoc. 2001 Oct;24(4):187-93. doi: 10.1007/s11357-001-0020-6. PMID: 23604884; PMCID: PMC3455297.
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Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype .

Plant physiology

Fluhr R, Lips SH, Sagi M.
PMID: 10364409
Plant Physiol. 1999 Jun;120(2):571-8. doi: 10.1104/pp.120.2.571.
Free PMC Article

The flacca tomato (Lycopersicon esculentum) mutant displays a wilty phenotype as a result of abscisic acid (ABA) deficiency. The Mo cofactor (MoCo)-containing aldehyde oxidases (AO; EC 1.2.3.1) are thought to play a role in the final oxidation step required...

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Fluhr R, Lips SH, Sagi M. Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype . Plant Physiol. 1999;120(2):571-8doi: 10.1104/pp.120.2.571.
Fluhr, R., Lips, S. H., & Sagi, M. (1999). Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype . Plant physiology, 120(2), 571-8. https://doi.org/10.1104/pp.120.2.571
Fluhr, et al. "Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype ." Plant physiology vol. 120,2 (1999): 571-8. doi: https://doi.org/10.1104/pp.120.2.571
Fluhr R, Lips SH, Sagi M. Aldehyde oxidase and xanthine dehydrogenase in a flacca tomato mutant with deficient abscisic acid and wilty phenotype . Plant Physiol. 1999 Jun;120(2):571-8. doi: 10.1104/pp.120.2.571. PMID: 10364409; PMCID: PMC59296.
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Biochemical characterization of the molybdenum cofactor mutants of Neurospora crassa: in vivo and in vitro reconstitution of NADPH-nitrate reductase activity.

Current genetics

Dunn-Coleman NS.
PMID: 24177997
Curr Genet. 1984 Oct;8(8):581-8. doi: 10.1007/BF00395703.

Molybdenum cofactor (MoCo) mutants of Neurospora crassa lack both NADPH-nitrate reductase and xanthine dehydrogenase activity. In vivo and in vitro studies to further characterize these mutants are now reported. The MoCo mutants nit-9A and nit-9B are capable of growing,...

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Dunn-Coleman NS. Biochemical characterization of the molybdenum cofactor mutants of Neurospora crassa: in vivo and in vitro reconstitution of NADPH-nitrate reductase activity. Curr Genet. 1984;8(8):581-8doi: 10.1007/BF00395703.
Dunn-Coleman, N. S. (1984). Biochemical characterization of the molybdenum cofactor mutants of Neurospora crassa: in vivo and in vitro reconstitution of NADPH-nitrate reductase activity. Current genetics, 8(8), 581-8. https://doi.org/10.1007/BF00395703
Dunn-Coleman, N S. "Biochemical characterization of the molybdenum cofactor mutants of Neurospora crassa: in vivo and in vitro reconstitution of NADPH-nitrate reductase activity." Current genetics vol. 8,8 (1984): 581-8. doi: https://doi.org/10.1007/BF00395703
Dunn-Coleman NS. Biochemical characterization of the molybdenum cofactor mutants of Neurospora crassa: in vivo and in vitro reconstitution of NADPH-nitrate reductase activity. Curr Genet. 1984 Oct;8(8):581-8. doi: 10.1007/BF00395703. PMID: 24177997.
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Showing 1 to 12 of 94 entries