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Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats.

The Journal of nutritional biochemistry

Meziani K, Benamouzig R, Mahé S, Martin A, Bouras M, Rautureau J, Tomé D.
PMID: 15539316
J Nutr Biochem. 1999 Jul;10(7):405-10. doi: 10.1016/s0955-2863(99)00019-4.

This study was performed to determine whether intestinal luminal polyamine concentrations are affected by a high soy protein diet when compared with a high casein diet or a normoprotein casein diet. We also determined the effects of these diets,...

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Meziani K, Benamouzig R, Mahé S, et al. Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats. J Nutr Biochem. 1999;10(7):405-10doi: 10.1016/s0955-2863(99)00019-4.
Meziani, K., Benamouzig, R., Mahé, S., Martin, A., Bouras, M., Rautureau, J., & Tomé, D. (1999). Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats. The Journal of nutritional biochemistry, 10(7), 405-10. https://doi.org/10.1016/s0955-2863(99)00019-4
Meziani, K, et al. "Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats." The Journal of nutritional biochemistry vol. 10,7 (1999): 405-10. doi: https://doi.org/10.1016/s0955-2863(99)00019-4
Meziani K, Benamouzig R, Mahé S, Martin A, Bouras M, Rautureau J, Tomé D. Effects of a high soy protein diet on intestinal polyamines and ornithine decarboxylase activity in rats. J Nutr Biochem. 1999 Jul;10(7):405-10. doi: 10.1016/s0955-2863(99)00019-4. PMID: 15539316.
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Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria.

Plant physiology

Birecka H, Birecki M, Cohen EJ, Bitonti AJ, McCann PP.
PMID: 16665870
Plant Physiol. 1988 Jan;86(1):224-30. doi: 10.1104/pp.86.1.224.

When tested for ornithine and arginine decarboxylases, pyrrolizidine alkaloid-bearing Senecio riddellii, S. longilobus (Compositae), and Crotalaria retusa (Leguminosae) plants exhibited only ornithine decarboxylase activity. This contrasts with previous studies of four species of pyrrolizidine alkaloid-bearing Heliotropium (Boraginaceae) in which...

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Birecka H, Birecki M, Cohen EJ, et al. Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria. Plant Physiol. 1988;86(1):224-30doi: 10.1104/pp.86.1.224.
Birecka, H., Birecki, M., Cohen, E. J., Bitonti, A. J., & McCann, P. P. (1988). Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria. Plant physiology, 86(1), 224-30. https://doi.org/10.1104/pp.86.1.224
Birecka, H, et al. "Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria." Plant physiology vol. 86,1 (1988): 224-30. doi: https://doi.org/10.1104/pp.86.1.224
Birecka H, Birecki M, Cohen EJ, Bitonti AJ, McCann PP. Ornithine decarboxylase, polyamines, and pyrrolizidine alkaloids in senecio and crotalaria. Plant Physiol. 1988 Jan;86(1):224-30. doi: 10.1104/pp.86.1.224. PMID: 16665870; PMCID: PMC1054458.
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Utilization of putrescine in tobacco cell lines resistant to inhibitors of polyamine synthesis.

Plant physiology

Hiatt A, Malmberg RL.
PMID: 16665927
Plant Physiol. 1988 Feb;86(2):441-6. doi: 10.1104/pp.86.2.441.

Three tobacco cell lines have been analyzed which are resistant to lethal inhibitors of either putrescine production or conversion of putrescine into polyamines. Free and conjugated putrescine pools, the enzymic activities (arginine, ornithine, and S-adenosylmethionine decarboxylases), and the growth...

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Hiatt A, Malmberg RL. Utilization of putrescine in tobacco cell lines resistant to inhibitors of polyamine synthesis. Plant Physiol. 1988;86(2):441-6doi: 10.1104/pp.86.2.441.
Hiatt, A., & Malmberg, R. L. (1988). Utilization of putrescine in tobacco cell lines resistant to inhibitors of polyamine synthesis. Plant physiology, 86(2), 441-6. https://doi.org/10.1104/pp.86.2.441
Hiatt, A, and Malmberg, R L. "Utilization of putrescine in tobacco cell lines resistant to inhibitors of polyamine synthesis." Plant physiology vol. 86,2 (1988): 441-6. doi: https://doi.org/10.1104/pp.86.2.441
Hiatt A, Malmberg RL. Utilization of putrescine in tobacco cell lines resistant to inhibitors of polyamine synthesis. Plant Physiol. 1988 Feb;86(2):441-6. doi: 10.1104/pp.86.2.441. PMID: 16665927; PMCID: PMC1054503.
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Effect of Exogenous Putrescine, Spermidine, and Spermine on K Uptake and H Extrusion through Plasmamembrane in Maize Root Segments.

Plant physiology

de Agazio M, Giardina MC, Grego S.
PMID: 16666098
Plant Physiol. 1988 May;87(1):176-8. doi: 10.1104/pp.87.1.176.

The action of exogenous polyamines (putrescine, spermidine, and spermine) on ;washing' and fusicoccin-stimulated K(+) uptake and H(+) extrusion through the plasmamembrane in maize (Zea mays L., hybrid line Plenus S 516) root apical segments was studied. The results showed...

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de Agazio M, Giardina MC, Grego S. Effect of Exogenous Putrescine, Spermidine, and Spermine on K Uptake and H Extrusion through Plasmamembrane in Maize Root Segments. Plant Physiol. 1988;87(1):176-8doi: 10.1104/pp.87.1.176.
de Agazio, M., Giardina, M. C., & Grego, S. (1988). Effect of Exogenous Putrescine, Spermidine, and Spermine on K Uptake and H Extrusion through Plasmamembrane in Maize Root Segments. Plant physiology, 87(1), 176-8. https://doi.org/10.1104/pp.87.1.176
de Agazio, M, et al. "Effect of Exogenous Putrescine, Spermidine, and Spermine on K Uptake and H Extrusion through Plasmamembrane in Maize Root Segments." Plant physiology vol. 87,1 (1988): 176-8. doi: https://doi.org/10.1104/pp.87.1.176
de Agazio M, Giardina MC, Grego S. Effect of Exogenous Putrescine, Spermidine, and Spermine on K Uptake and H Extrusion through Plasmamembrane in Maize Root Segments. Plant Physiol. 1988 May;87(1):176-8. doi: 10.1104/pp.87.1.176. PMID: 16666098; PMCID: PMC1054720.
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An Improved Method for Analysis of Polyamines in Plant Tissue by Precolumn Derivatization with o-Phthalaldehyde and Separation by High Performance Liquid Chromatography.

Plant physiology

Corbin JL, Marsh BH, Peters GA.
PMID: 16666789
Plant Physiol. 1989 Jun;90(2):434-9. doi: 10.1104/pp.90.2.434.

An improved high-performance liquid-chromatographic method was developed for estimation of polyamines in crude plant extracts. Polyamines were derivatized with o-phthalaldehyde and mercaptoethanol (OPT). The fluorescent derivatives were eluted from a C(18) column with the dimethylcyclohexylamine-phosphate buffer derived by T....

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Corbin JL, Marsh BH, Peters GA. An Improved Method for Analysis of Polyamines in Plant Tissue by Precolumn Derivatization with o-Phthalaldehyde and Separation by High Performance Liquid Chromatography. Plant Physiol. 1989;90(2):434-9doi: 10.1104/pp.90.2.434.
Corbin, J. L., Marsh, B. H., & Peters, G. A. (1989). An Improved Method for Analysis of Polyamines in Plant Tissue by Precolumn Derivatization with o-Phthalaldehyde and Separation by High Performance Liquid Chromatography. Plant physiology, 90(2), 434-9. https://doi.org/10.1104/pp.90.2.434
Corbin, J L, et al. "An Improved Method for Analysis of Polyamines in Plant Tissue by Precolumn Derivatization with o-Phthalaldehyde and Separation by High Performance Liquid Chromatography." Plant physiology vol. 90,2 (1989): 434-9. doi: https://doi.org/10.1104/pp.90.2.434
Corbin JL, Marsh BH, Peters GA. An Improved Method for Analysis of Polyamines in Plant Tissue by Precolumn Derivatization with o-Phthalaldehyde and Separation by High Performance Liquid Chromatography. Plant Physiol. 1989 Jun;90(2):434-9. doi: 10.1104/pp.90.2.434. PMID: 16666789; PMCID: PMC1061742.
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Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa).

Plant physiology

Margosiak SA, Dharma A, Bruce-Carver MR, Gonzales AP, Louie D, Kuehn GD.
PMID: 16667270
Plant Physiol. 1990 Jan;92(1):88-96. doi: 10.1104/pp.92.1.88.

Extracts prepared from floral meristematic tissue of alfalfa (Medicago sativa L.) were investigated for expression of the enzyme transglutaminase in order to identify the major protein substrate for transglutaminase-directed modifications among plant proteins. The large polymorphic subunits of ribulose...

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Margosiak SA, Dharma A, Bruce-Carver MR, et al. Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa). Plant Physiol. 1990;92(1):88-96doi: 10.1104/pp.92.1.88.
Margosiak, S. A., Dharma, A., Bruce-Carver, M. R., Gonzales, A. P., Louie, D., & Kuehn, G. D. (1990). Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa). Plant physiology, 92(1), 88-96. https://doi.org/10.1104/pp.92.1.88
Margosiak, S A, et al. "Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa)." Plant physiology vol. 92,1 (1990): 88-96. doi: https://doi.org/10.1104/pp.92.1.88
Margosiak SA, Dharma A, Bruce-Carver MR, Gonzales AP, Louie D, Kuehn GD. Identification of the Large Subunit of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase as a Substrate for Transglutaminase in Medicago sativa L. (Alfalfa). Plant Physiol. 1990 Jan;92(1):88-96. doi: 10.1104/pp.92.1.88. PMID: 16667270; PMCID: PMC1062252.
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Polyamines, hydroxycinnamoylputrescines, and root formation in leaf explants of tobacco cultivated in vitro: effects of the suicide inhibitors of putrescine synthesis.

Plant physiology

Burtin D, Martin-Tanguy J, Paynot M, Carré M, Rossin N.
PMID: 16667631
Plant Physiol. 1990 Aug;93(4):1398-404. doi: 10.1104/pp.93.4.1398.

In vitro formation of roots is obtained directly, without intermediate growth of callus, from foliar explants of a tobacco (Nicotiana tabacum) plant cultured on Murashige and Skoog medium containing IAA. Auxin-induced root formation was accompanied by significant changes in...

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Burtin D, Martin-Tanguy J, Paynot M, et al. Polyamines, hydroxycinnamoylputrescines, and root formation in leaf explants of tobacco cultivated in vitro: effects of the suicide inhibitors of putrescine synthesis. Plant Physiol. 1990;93(4):1398-404doi: 10.1104/pp.93.4.1398.
Burtin, D., Martin-Tanguy, J., Paynot, M., Carré, M., & Rossin, N. (1990). Polyamines, hydroxycinnamoylputrescines, and root formation in leaf explants of tobacco cultivated in vitro: effects of the suicide inhibitors of putrescine synthesis. Plant physiology, 93(4), 1398-404. https://doi.org/10.1104/pp.93.4.1398
Burtin, D, et al. "Polyamines, hydroxycinnamoylputrescines, and root formation in leaf explants of tobacco cultivated in vitro: effects of the suicide inhibitors of putrescine synthesis." Plant physiology vol. 93,4 (1990): 1398-404. doi: https://doi.org/10.1104/pp.93.4.1398
Burtin D, Martin-Tanguy J, Paynot M, Carré M, Rossin N. Polyamines, hydroxycinnamoylputrescines, and root formation in leaf explants of tobacco cultivated in vitro: effects of the suicide inhibitors of putrescine synthesis. Plant Physiol. 1990 Aug;93(4):1398-404. doi: 10.1104/pp.93.4.1398. PMID: 16667631; PMCID: PMC1062686.
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Polyamine biosynthesis and inhibition in Trichomonas vaginalis.

Parasitology today (Personal ed.)

Yarlett N.
PMID: 15463030
Parasitol Today. 1988 Dec;4(12):357-60. doi: 10.1016/0169-4758(88)90007-5.

Polyomines - particularly putrescine, spermidine and spermine - are ubiquitous components of eukaryote and most prokaryote cells, and are essential for optimal cell proliferation. But since routes of polyamine synthesis may differ, for example between parasites and their hosts,...

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Yarlett N. Polyamine biosynthesis and inhibition in Trichomonas vaginalis. Parasitol Today. 1988;4(12):357-60doi: 10.1016/0169-4758(88)90007-5.
Yarlett, N. (1988). Polyamine biosynthesis and inhibition in Trichomonas vaginalis. Parasitology today (Personal ed.), 4(12), 357-60. https://doi.org/10.1016/0169-4758(88)90007-5
Yarlett, N. "Polyamine biosynthesis and inhibition in Trichomonas vaginalis." Parasitology today (Personal ed.) vol. 4,12 (1988): 357-60. doi: https://doi.org/10.1016/0169-4758(88)90007-5
Yarlett N. Polyamine biosynthesis and inhibition in Trichomonas vaginalis. Parasitol Today. 1988 Dec;4(12):357-60. doi: 10.1016/0169-4758(88)90007-5. PMID: 15463030.
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Relation of polyamine biosynthesis to the initiation of sprouting in potato tubers.

Plant physiology

Kaur-Sawhney R, Shih LM, Galston AW.
PMID: 16662219
Plant Physiol. 1982 Feb;69(2):411-5. doi: 10.1104/pp.69.2.411.

The polyamines putrescine, spermidine, and spermine and their biosynthetic enzymes arginine decarboxylase, ornithine decarboxylase and S-adenosyl-l-methionine decarboxylase are present in all parts of dormant potato (Solanum tuberosum L.) tubers. They are equally distributed among the buds of apical and...

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Kaur-Sawhney R, Shih LM, Galston AW. Relation of polyamine biosynthesis to the initiation of sprouting in potato tubers. Plant Physiol. 1982;69(2):411-5doi: 10.1104/pp.69.2.411.
Kaur-Sawhney, R., Shih, L. M., & Galston, A. W. (1982). Relation of polyamine biosynthesis to the initiation of sprouting in potato tubers. Plant physiology, 69(2), 411-5. https://doi.org/10.1104/pp.69.2.411
Kaur-Sawhney, R, et al. "Relation of polyamine biosynthesis to the initiation of sprouting in potato tubers." Plant physiology vol. 69,2 (1982): 411-5. doi: https://doi.org/10.1104/pp.69.2.411
Kaur-Sawhney R, Shih LM, Galston AW. Relation of polyamine biosynthesis to the initiation of sprouting in potato tubers. Plant Physiol. 1982 Feb;69(2):411-5. doi: 10.1104/pp.69.2.411. PMID: 16662219; PMCID: PMC426220.
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Assaying ornithine and arginine decarboxylases in some plant species.

Plant physiology

Birecka H, Bitonti AJ, McCann PP.
PMID: 16664441
Plant Physiol. 1985 Oct;79(2):509-14. doi: 10.1104/pp.79.2.509.

A release of (14)CO(2) not related to ornithine decarboxylase activity was found in crude leaf extracts from Lycopersicon esculentum, Avena sativa, and especially from the pyrrolizidine alkaloid-bearing Heliotropium angiospermum when incubated with [1-(14)C]- or [U-(14)C]ornithine. The total (14)CO(2) produced...

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Birecka H, Bitonti AJ, McCann PP. Assaying ornithine and arginine decarboxylases in some plant species. Plant Physiol. 1985;79(2):509-14doi: 10.1104/pp.79.2.509.
Birecka, H., Bitonti, A. J., & McCann, P. P. (1985). Assaying ornithine and arginine decarboxylases in some plant species. Plant physiology, 79(2), 509-14. https://doi.org/10.1104/pp.79.2.509
Birecka, H, et al. "Assaying ornithine and arginine decarboxylases in some plant species." Plant physiology vol. 79,2 (1985): 509-14. doi: https://doi.org/10.1104/pp.79.2.509
Birecka H, Bitonti AJ, McCann PP. Assaying ornithine and arginine decarboxylases in some plant species. Plant Physiol. 1985 Oct;79(2):509-14. doi: 10.1104/pp.79.2.509. PMID: 16664441; PMCID: PMC1074916.
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Release of Calcium from Suspension-Cultured Glycine max Cells by Chitosan, Other Polycations, and Polyamines in Relation to Effects on Membrane Permeability.

Plant physiology

Young DH, Kauss H.
PMID: 16663285
Plant Physiol. 1983 Nov;73(3):698-702. doi: 10.1104/pp.73.3.698.

Treatment with chitosan of suspension-cultured Glycine max cells labeled with (45)Ca(2+) caused a rapid release of calcium, which was complete much earlier than the chitosan-induced leakage of intracellular electrolytes and probably reflects calcium loss primarily from the cell wall...

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Young DH, Kauss H. Release of Calcium from Suspension-Cultured Glycine max Cells by Chitosan, Other Polycations, and Polyamines in Relation to Effects on Membrane Permeability. Plant Physiol. 1983;73(3):698-702doi: 10.1104/pp.73.3.698.
Young, D. H., & Kauss, H. (1983). Release of Calcium from Suspension-Cultured Glycine max Cells by Chitosan, Other Polycations, and Polyamines in Relation to Effects on Membrane Permeability. Plant physiology, 73(3), 698-702. https://doi.org/10.1104/pp.73.3.698
Young, D H, and Kauss, H. "Release of Calcium from Suspension-Cultured Glycine max Cells by Chitosan, Other Polycations, and Polyamines in Relation to Effects on Membrane Permeability." Plant physiology vol. 73,3 (1983): 698-702. doi: https://doi.org/10.1104/pp.73.3.698
Young DH, Kauss H. Release of Calcium from Suspension-Cultured Glycine max Cells by Chitosan, Other Polycations, and Polyamines in Relation to Effects on Membrane Permeability. Plant Physiol. 1983 Nov;73(3):698-702. doi: 10.1104/pp.73.3.698. PMID: 16663285; PMCID: PMC1066533.
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Stabilization of Oat Leaf Protoplasts through Polyamine-mediated Inhibition of Senescence.

Plant physiology

Altman A, Kaur-Sawhney R, Galston AW.
PMID: 16660139
Plant Physiol. 1977 Oct;60(4):570-4. doi: 10.1104/pp.60.4.570.

Protoplasts isolated from Avena sativa L. leaves undergo progressive senescence when incubated aseptically in 0.6 m mannitol with or without added nutrients. This senescence is manifested by morphological deterioration and ultimate lysis of protoplasts, by a decrease in incorporation...

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Altman A, Kaur-Sawhney R, Galston AW. Stabilization of Oat Leaf Protoplasts through Polyamine-mediated Inhibition of Senescence. Plant Physiol. 1977;60(4):570-4doi: 10.1104/pp.60.4.570.
Altman, A., Kaur-Sawhney, R., & Galston, A. W. (1977). Stabilization of Oat Leaf Protoplasts through Polyamine-mediated Inhibition of Senescence. Plant physiology, 60(4), 570-4. https://doi.org/10.1104/pp.60.4.570
Altman, A, et al. "Stabilization of Oat Leaf Protoplasts through Polyamine-mediated Inhibition of Senescence." Plant physiology vol. 60,4 (1977): 570-4. doi: https://doi.org/10.1104/pp.60.4.570
Altman A, Kaur-Sawhney R, Galston AW. Stabilization of Oat Leaf Protoplasts through Polyamine-mediated Inhibition of Senescence. Plant Physiol. 1977 Oct;60(4):570-4. doi: 10.1104/pp.60.4.570. PMID: 16660139; PMCID: PMC542665.
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