Academic literature on the topic 'Purine catabolism'
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Journal articles on the topic "Purine catabolism"
Tomlinson, Patricia Tolson, and Carol J. Lovatt. "Nucleotide Metabolism in ‘Washington’ Navel Orange Fruit: I. Pathways of Synthesis and Catabolism." Journal of the American Society for Horticultural Science 112, no. 3 (May 1987): 529–35. http://dx.doi.org/10.21273/jashs.112.3.529.
Full textXi, Hualin, Barbara L. Schneider, and Larry Reitzer. "Purine Catabolism in Escherichia coliand Function of Xanthine Dehydrogenase in Purine Salvage." Journal of Bacteriology 182, no. 19 (October 1, 2000): 5332–41. http://dx.doi.org/10.1128/jb.182.19.5332-5341.2000.
Full textSun, Runbin, Jingqiu Huang, Na Yang, Jun He, Xiaoyi Yu, Siqi Feng, Yuan Xie, Guangji Wang, Hui Ye, and Jiye Aa. "Purine Catabolism Shows a Dampened Circadian Rhythmicity in a High-fat Diet-Induced Mouse Model of Obesity." Molecules 24, no. 24 (December 10, 2019): 4524. http://dx.doi.org/10.3390/molecules24244524.
Full textYin, Yuling, Riko Katahira, and Hiroshi Ashihara. "Metabolism of Purine Alkaloids and Xanthine in Leaves of Maté (Ilex paraguariensis)." Natural Product Communications 10, no. 5 (May 2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000503.
Full textMuzychka, Oksana, Olexandr Kobzar, Oleg Shablykin, Volodymyr Brovarets, and Andriy Vovk. "5-Substituted N-(9H-purin-6-yl)-1,2-oxazole-3-carboxamides as xanthine oxidase inhibitors." Ukr. Bioorg. Acta 2020, Vol. 15, N1 15, no. 1 (June 30, 2020): 20–25. http://dx.doi.org/10.15407/bioorganica2020.01.020.
Full textItakura, M., N. Maeda, and K. Yamashita. "Increased rate of purine biosynthesis in rat liver after bilateral adrenalectomy." American Journal of Physiology-Endocrinology and Metabolism 251, no. 4 (October 1, 1986): E373—E378. http://dx.doi.org/10.1152/ajpendo.1986.251.4.e373.
Full textPizzichin, M., M. L. Pandolfi, L. Terzuoli, L. Arezzini, and R. Pagani. "Purine nucleotide catabolism in rat liver." Biochemical Society Transactions 21, no. 2 (May 1, 1993): 189S. http://dx.doi.org/10.1042/bst021189s.
Full textHADANO, SHINJI, SATOSHI SAKAI, MASASHI OGASAWARA, and AKIRA ITO. "EFFECTS OF EXERCISE INTENSITY ON PURINE CATABOLISM." Japanese Journal of Physical Fitness and Sports Medicine 37, no. 3 (1988): 225–33. http://dx.doi.org/10.7600/jspfsm1949.37.225.
Full textFelici, C., I. Ciari, L. Terzuoli, B. Porcelli, C. Setacci, M. Giubbolini, and E. Marinello. "Purine Catabolism in Advanced Carotid Artery Plaque." Nucleosides, Nucleotides and Nucleic Acids 25, no. 9-11 (June 2006): 1291–94. http://dx.doi.org/10.1080/15257770600890772.
Full textVoloshchuk, Oksana, Halyna Kopylchuk, and Andriana Plytus. "Activity of purine nucleotide catabolic enzymes in the liver of rats under conditions of nutritional imbalance." Biolohichni systemy 12, no. 2 (December 23, 2020): 119–24. http://dx.doi.org/10.31861/biosystems2020.02.119.
Full textDissertations / Theses on the topic "Purine catabolism"
Le, Tissier Paul Roussel. "The biochemical genetics of purine catabolism in mice." Thesis, University of Reading, 1990. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.236393.
Full textKavianipour, Mohammad. "Myocardial energy metabolism in ischemic preconditioning, role of adenosine catabolism." Doctoral thesis, Umeå University, Public Health and Clinical Medicine, 2002. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-14.
Full textBrief episodes of ischemia and reperfusion render the myocardium more resistant to necrosis from a subsequent, otherwise lethal ischemic insult. This phenomenon is called ischemic preconditioning(IP). Today, much is known about the signalling pathways involved in IP; however, the details of the final steps leading to cardioprotection, remain elusive. Adenosine (a catabolite of ATP) plays a major role in the signalling pathways of IP. Following IP there is an unexplained discrepancy between an increased adenosine production (evidenced by increased 5’-nucleotidase activity) and the successively lower adenosine levels observed in the interstitial space. We propose that this discrepancy in adenosine production vs. availability may be due to an increased metabolic utilisation of adenosine by the IP myocardium. According to our hypothesis, IP induces/activates a metabolic pathway involving deamination of adenosine to inosine. Inosine is further catalysed (in presence of Pi) to hypoxanthine and ribose-1-phosphate. Ribose-1-phosphate can be converted to ribose-5-phosphate in a phosphoribomutase reaction. Ribose-5-phosphate is an intermediate of the hexose monophosphate pathway also operative under anaerobic conditions. Hence the ribose moiety of adenosine can be utilised to generate pyruvate and ultimately ATP (via lactate formation) n.b. without any initial ATP investment. Such cost-effective adenosine utilisation may at least partly explain the cardioprotective effect of IP. Objectives & Methods: In the current studies we investigated the role of adenosine metabolism according to the suggested metabolic pathway by addition of adenosine and inhibition of its metabolism during IP as well as by comparing tissue and interstitial levels of key energy-metabolites following different protocols of IP. Furthermore, we studied the importance of the IP protocol with regard to the number of ischemia and reperfusion cycles for the cardioprotective effect of IP. In addition, the validity of the microdialysis technique for experimental in vivo studies of myocardial energy metabolism was evaluated. For these purposes the microdialysis technique, tissue biopsies, and planimetric infarct size estimation in an open chest porcine heart-model was used. Results: Addition of adenosine via microdialysis probes enhanced the interstitial release of inosine, hypoxanthine and lactate in the myocardium of IP-subjects during prolonged ischemia. This finding did not occur in non-preconditioned subjects. Similar addition of deoxyadenosine a non-metabolizable adenosine receptor-agonist, did not evoke the same metabolic response. Purine nucleoside phosphorylase (PNP) is responsible for the conversion of inosine to hypoxanthine being a key enzyme in the above mentioned metabolic pathway. Inclusion of 8' aminoguanosine (a competitive inhibitor of PNP) decreased interstitial hypoxanthine release (as a token of PNP inhibition) and increased the release of taurine (marker of cellular injury) in the ischemic IP myocardium. Addition of inosine (a natural substrate of PNP) reverted these changes. Four IP cycles protected the heart more than one IP cycle as evidenced by morphometric and energy-metabolic data.Proportionally more hypoxanthine was found in the myocardium of IP subjects during prolonged ischemia. The ratio of tissue levels of inosine/hypoxanthine (used as an indicator of PNP activity) was significantly smaller in the IP groups. In addition, myocardial interstitial levels of energy-related metabolites (lactate, adenosine, inosine, and hypoxanthine) obtained by the microdialysis technique correlated with tissue biopsy levels of corresponding metabolites. Conclusions: IP activated a metabolic pathway favouring metabolism of exogenous adenosine to inosine, hypoxanthine and eventually lactate. Inhibition of adenosine metabolism following IP (via inhibition of PNP-activity resulted in enhanced cellular injury.
PNP-activity is proportionally higher in IP-myocardium. Metabolic utilisation of adenosine in IP-myocardium (as outlined above) may represent a costeffective way to produce ATP and at least partly explain the cardioprotective effect of IP. IP protects the myocardium in a graded fashion. Furthermore, we confirmed the validity of the microdialysis technique (in the current setting) for studying dynamic changes of myocardial energy metabolism.
Baccolini, Chiara [Verfasser]. "Analysis of in vivo purine nucleotide catabolism in Arabidopsis thaliana with focus on nucleoside hydrolase 2 / Chiara Baccolini." Hannover : Gottfried Wilhelm Leibniz Universität Hannover, 2019. http://d-nb.info/1193177146/34.
Full textHuynh, Hanh Kim. "Physiological, ultrastructural and cytochemical studies on the utilization of various intermediates of the purine catabolism pathway as sole sources of nitrogen by marine phytoplankters." Thesis, University of British Columbia, 1989. http://hdl.handle.net/2429/27491.
Full textScience, Faculty of
Botany, Department of
Graduate
Lee, Hakjoo. "Nitrogen regulation of the purine catabolic genes in Neurospora crassa /." The Ohio State University, 1990. http://rave.ohiolink.edu/etdc/view?acc_num=osu1487681148541111.
Full textCecchetto, Gianna. "Catabolisme de purines chez Aspergillus nidulans : caractérisation du transporteur AzgA : analyse de la fixation à l'ADN de l'activateur transcriptionnel UaY." Paris 11, 2003. http://www.theses.fr/2003PA112331.
Full textAt least three permeases are involved in purine transport in Aspergillus nidulans. The AzgA protein is the main transporter for adenine and hypoxanthine and UapA transport xanthine and uric acid. The UapC protein is a low-capacity transporter for all natural purines. Expression of uapA and uapC genes in mycelium is induced by purines and repressed by ammonium through the action of the pathway-specific UaY regulator and the general GATA factor AreA, respectively. Here we present the characterisation of azgA gene and its protein product. AzgA protein defines an UapA-UapC distant sub-family of Xanthine/uracil permeases family. AzgA expression is induced by uric acid and repressed by ammonium. During the isotropic growth phase of conidial germination, the expression of the three purine transporter genes are induced by uric acid. The ammonium repression is very low. Transcriptional activation occurs in the absence of purine induction and independently of the nitrogen and carbon source present in the medium. This work establishes the presence of a novel system triggering purine transporter transcription during germination. We have studied the UaY-DNA interactions. UaY, a Zn binuclear cluster transcription factor, binds as a dimmer through UaY(103-147) domain. Phe112 is important for the dimmeric structure stabilisation, which is diminished in a F112I mutant. This modification reduces the transcription activation of almost five genes under UaY control as well as its affinity to its targets. Revertants re-establish wild type phenotype by altering the interactions between this activator and its DNA targets or by affecting the activation function
RIBARD, CARIN. "Etude de la regulation du catabolisme des purines chez aspergillus nidulans : - clonage et caracterisation moleculaire de oxpa. - caracterisation moleculaire de nada." Paris 11, 1999. http://www.theses.fr/1999PA112379.
Full textOESTREICHER, NATHALIE. "Etude moleculaire de la regulation du catabolisme des purines chez aspergillus nidulans : caracterisation du gmene de l'urate oxydase. analyse fonctionnelle du regulateur positif." Paris 11, 1991. http://www.theses.fr/1991PA112276.
Full textCasartelli, Alberto. "Purine Catabolism in Wheat: Source of Nutrients and Protective Metabolites." Thesis, 2018. http://hdl.handle.net/2440/123271.
Full textThesis (Ph.D.) -- University of Adelaide, School of Agriculture, Food & Wine, 2018
Book chapters on the topic "Purine catabolism"
Cohen, Amos, and Jerzy Barankiewicz. "Purine Ribonucleotide and Deoxyribonucleotide Catabolism in Lymphocytes." In Purine and Pyrimidine Metabolism in Man V, 561–65. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5104-7_94.
Full textTerzuoli, Lucia, Maria Pizzichini, Anna Di Stefano, Brunetta Porcelli, Antonella Tabucchi, and Roberto Pagani. "Purine Nucleotide Catabolism in Rat Liver After Castration." In Advances in Experimental Medicine and Biology, 297–300. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4899-2638-8_67.
Full textBontemps, F., G. Van den Berghe, and H. G. Hers. "Pathways of Adenine Nucleotide Catabolism in Human Erythrocytes." In Purine and Pyrimidine Metabolism in Man V, 329–36. New York, NY: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_53.
Full textSchopf, Gerhard, Michael Havel, Roland Fasol, and Mathias M. Müller. "Enzyme Activities of Purine Catabolism and Salvage in Human Muscle Tissue." In Purine and Pyrimidine Metabolism in Man V, 507–9. New York, NY: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_78.
Full textBarankiewicz, Jerzy, and Amos Cohen. "Ethanol Induced Nucleotide Catabolism in Mouse T Lymphoblastoid Cells in Vitro." In Purine and Pyrimidine Metabolism in Man V, 227–30. New York, NY: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_34.
Full textHelland, S., and P. M. Ueland. "Determination of S-Adenosylhomocysteine in Tissues Following Pharmacological Inhibition of S-Adenosylhomocysteine Catabolism." In Purine and Pyrimidine Metabolism in Man V, 663–66. New York, NY: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_103.
Full textvan Waeg, Geert, Frank Niklasson, and Carl-Henric de Verdier. "Deamination of Guanine to Xanthine: A Metabolic Pathway of Underestimated Importance in Human Purine Catabolism?" In Purine and Pyrimidine Metabolism in Man V, 425–30. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5104-7_70.
Full textKather, H. "Beta Adrenergic Receptor Mediated Stimulation of Adenine Nucleotide Catabolism and Purine Release in Human Adipocytes." In Purines in Cellular Signaling, 120–25. New York, NY: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4612-3400-5_20.
Full textWortmann, Robert L., Judith A. Veum, and John W. Rachow. "Purine Catabolic Enzymes in Human Synovial Fluids." In Advances in Experimental Medicine and Biology, 393–98. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-5673-8_64.
Full textGojkovic, Zoran, Silvia Paracchini, and Jure Piskur. "A New Model Organism for Studying the Catabolism of Pyrimidines and Purines." In Advances in Experimental Medicine and Biology, 475–79. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5381-6_94.
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