Оценка засухоустойчивости сои по активности ферментов-антиоксидантов и альдегидоксидазы / Антиоксидант-ферменттер және альдегидоксидаза бойынша сояның құрғақшылыққа төзімділігін бағалау
Ключевые слова:
индексы засухоустойчивости, активные формы кислорода, ферменты-антиоксиданты, альдегидоксидаза, құрғақшылыққа төзімділік көрсеткіштері, оттегінің белсенді формалары, антоксидант-ферменттер, альдегидоксидаза.Аннотация
Осы жұмыстың мақсаты соя генотиптерінің құрғақшылыққа төзімділігін онтогенездің ерте сатысында скринингтеу үшін энзиматикалық белсенділік деңгейінде антиоксидантты ферменттер – пероксидаза (ПОД), супероксиддисмутаза (СОД) және альдегидоксидазаны (АО) зерттеу болып табылады. Зерттеу обьектісі ретінде әлемдік коллекциядан Glycine max L. соя культурасының құрғақшылыққа жоғары төзімділік қасиетіне ие сортүлгілері: Устя (Украина), K589109 (Ресей), K583583 HMAS 84 (АҚШ) алынды. Бұл сорттар ультражылдампісетін, вегетация кезеңі 85-95 күн болатын топқа жатады. Стандарт ретінде отандық коллекциядан - жылдампісетін Алматы сорты қолданылды. Суғарылған және құрғақшылық жағдайындағы соя жапырақтарының СОД, ПОД және АО ферментативті белсенділігін анықтау су жетіспеушілкке аса сезімтал екі репродуктивті фаза– гүлдену R1 және бұршақтануда R5 жүргізілді. СОД, ПОД және АО ферментативті белсенділігін анықтау нәтижесі қазақстандық Алматы және К583583(АҚШ) сорттарының құрғақшылыққа төзімді екенін көрсетті. Целью данной работы являлось изучение ферментов-антиоксидантов – пероксидазы (ПОД), супероксиддисмутазы (СОД) и альдегидоксидазы (АО) на уровне энзиматической активности для скрининга засухоустойчивости генотипов сои на ранних этапах онтогенеза. Объектами исследования служили 4 сортообразца культурной сои Glycine max L. из мировой коллекции, по предварительным данным обладающие признаками засухоустойчивости: сорта Устя (Украина), K 589109(Россия), K583583 HMAS 84 (США), и относящиеся к ультраскороспелой группе с периодом вегетации 85-95 дней. В качестве стандарта был использован сорт отечественной селекции скороспелый Алматы. Определение ферментативной активности СОД, ПОД и АО в листьях сои было проведено в условиях полива и засухи в двух репродуктивных фазах вегетации, наиболее чувствительных к дефициту влаги – в фазе цветения R1 и налива бобов R5. По результатам определения ферментативной активности СОД, ПОД и АО наибольшую засухоустойчивость проявили казахстанский сорт Алматы и К583583(США).Библиографические ссылки
Литература
1. Tardieu F. Plant tolerance to water deficit: physical limits and possibilities for progress // Comp. Rend. Geosci. –2005. –Vol. 337.–P. 57-67.
2. Fehr W.R., Caviness C.E., Burmood O.T. and Pennington J.S. Stage of development description for soybeans Glycine max(L.) // Merril. Crop Sci. – Vol.11. – P. 929-931.
3. Chaves M.M., Oliveira M.M. Mechanisms underlying plant resilience to water deficits: prospects for water-saving agriculture // J.Exp. Bot. –2004. –V. 55. –No.55. –P.2365-2384.
4. Колупаев Ю.Е., Карпец Ю.В. Формирование адаптивных реакций растений на действие абиотических стрессоров. – Киев: Основа, 2010. – 351 с.
5. Maevskaya S.N., Nikolaeva M.K. Response of Antioxidant and Osmoprotective Systems of Wheat Seedlings to Drought and Rehydration. // Russian Journal of Plant Physiology. – 2013.–V. 60. – No.3. –Р.351–359.
6. Varga B., Janda T., La´szlo´ E., Veisz O. Influence of abiotic stresses on the antioxidant enzyme activity of cereals. // ActaPhysiol Plant. –2012.–Vol.34. –Р.849–858.
7. Helena M. Carvalho C. Drought stress and reactive oxygen species. Production, scavenging and signaling // Plant Signal Behav. – 2008. – Vol. 3. – P.156-165.
8. Suzuki N, Mittler R. Reactive oxygen species and temperature stresses: A delicate balance between signaling and destruction // Physiol. Plant. – 2006. – Vol.. 126. – P. 45-51.
9. Walker-Simmons M., Kudrna D.A., Warner RL. Reduced accumulation of ABA during water stress in a molybdenum cofactor mutant of barley // Plant Physiol. –1988. –Vol. 90. –P. 728-733
10. KoshibaT., SaitoE., OnoN., YamamotoN., SatoM. Purification and properties of flavin and molybdenum-containing aldehyde oxidase from coleoptiles of maize // Plant Physiol. –1996. – Vol.110. –P.781-789.
11. Beauchamp C., Fridovich J. Superoxide Dismutase: Improved Assays and an Assay Applicable to Acrylamide Gels // Anal. Biochem. –1971.–Vol. 44. –P. 276-287.
12. Лебедева О.В., Угарова Н.Н., Березин И.В. Кинетическое изучение реакции окисления о-дианизидина Н2О2 в присутствии пероксидазы хрена // Биохимия. –1977.–Т.42. – С.1372-1379.
13. Rothe G.M. Aldehyde oxidase isoenzymes (EC 1.2.3.1) in potato tubers (Solanumtuberosum). //Plant Cell Physiol. –1974.–Vol.15.–Р.493-499.
14. Laemmli K. Cleavage of structural proteins during the assembly of the headof bacteriophage // Nature. –1970. –Vol.4. – №227. –P.680-685.
15. Oliver H. Lowry, Nira J. Rosebrough, A.Lewis Farr and Rose J. Randall Protein measurement with the folin phenol reagent // J. Biol. Chem. –1951. –Vol.193. – P. 265-275.
References
1. Tardieu F. Plant tolerance to water deficit: physical limits and possibilities for progress // Comp. Rend. Geosci. –2005. –Vol. 337.–P. 57-67.
2. Fehr W.R., Caviness C.E., Burmood O.T. and Pennington J.S. Stage of development description for soybeans Glycine max(L.) // Merril. Crop Sci. – Vol.11. – P. 929-931.
3. Chaves M.M., Oliveira M.M. Mechanisms underlying plant resilience to water deficits: prospects for water-saving agriculture // J.Exp. Bot. –2004. –V. 55. –No.55. –P.2365-2384.
4. Kolupaev Y.E., Karpets Y.V. Formation of adaptive responses of plants to abiotic stressors action. –Kiev: Osnova, 2010. – 351 p.
5. Maevskaya S.N., Nikolaeva M.K. Response of Antioxidant and Osmoprotective Systems of Wheat Seedlings to Drought and Rehydration. // Russian Journal of Plant Physiology. – 2013.–V. 60. – No.3. –Р.351–359.
6. Varga B., Janda T., La´szlo´ E., Veisz O. Influence of abiotic stresses on the antioxidant enzyme activity of cereals. // ActaPhysiol Plant. –2012.–Vol.34. –Р.849–858.
7. Helena M. Carvalho C. Drought stress and reactive oxygen species. Production, scavenging and signaling // Plant Signal Behav. – 2008. – Vol. 3. – P.156-165.
8. Suzuki N, Mittler R. Reactive oxygen species and temperature stresses: A delicate balance between signaling and destruction // Physiol. Plant. – 2006. – Vol. 126. – P. 45-51.
9. Walker-Simmons M., Kudrna D.A., Warner RL. Reduced accumulation of ABA during water stress in a molybdenum cofactor mutant of barley // Plant Physiol. –1988. – Vol. 90. –P. 728-733
10. KoshibaT., SaitoE., OnoN., YamamotoN., SatoM. Purification and properties of flavin and molybdenum-containing aldehyde oxidase from coleoptiles of maize // Plant Physiol. –1996. – Vol.110. –P.781-789.
11. Beauchamp C., Fridovich J. Superoxide Dismutase: Improved Assays and an Assay Applicable to Acrylamide Gels // Anal. Biochem. –1971.–Vol. 44. –P. 276-287.
12. Lebedev O.V., Ugarov N.N., Berezin I.V. Kinetic study of the oxidation reaction of o-dianisidine in the presence of H2O2 horseradish peroxidase // Biochemistry. – 1977. – Vol.42.– P.1372-1379.
13. Rothe G.M. Aldehyde oxidase isoenzymes (EC 1.2.3.1) in potato tubers (Solanumtuberosum). //Plant Cell Physiol. –1974.–Vol.15.–Р.493-499.
14. Laemmli K. Cleavage of structural proteins during the assembly of the headof bacteriophage // Nature. –1970. –Vol..4. – №227. –P.680-685.
15. Oliver H. Lowry, Nira J. Rosebrough, A.Lewis Farr and Rose J. Randall Protein measurement with the folin phenol reagent // J. Biol. Chem. –1951. –Vol.193. – P. 265-275.
1. Tardieu F. Plant tolerance to water deficit: physical limits and possibilities for progress // Comp. Rend. Geosci. –2005. –Vol. 337.–P. 57-67.
2. Fehr W.R., Caviness C.E., Burmood O.T. and Pennington J.S. Stage of development description for soybeans Glycine max(L.) // Merril. Crop Sci. – Vol.11. – P. 929-931.
3. Chaves M.M., Oliveira M.M. Mechanisms underlying plant resilience to water deficits: prospects for water-saving agriculture // J.Exp. Bot. –2004. –V. 55. –No.55. –P.2365-2384.
4. Колупаев Ю.Е., Карпец Ю.В. Формирование адаптивных реакций растений на действие абиотических стрессоров. – Киев: Основа, 2010. – 351 с.
5. Maevskaya S.N., Nikolaeva M.K. Response of Antioxidant and Osmoprotective Systems of Wheat Seedlings to Drought and Rehydration. // Russian Journal of Plant Physiology. – 2013.–V. 60. – No.3. –Р.351–359.
6. Varga B., Janda T., La´szlo´ E., Veisz O. Influence of abiotic stresses on the antioxidant enzyme activity of cereals. // ActaPhysiol Plant. –2012.–Vol.34. –Р.849–858.
7. Helena M. Carvalho C. Drought stress and reactive oxygen species. Production, scavenging and signaling // Plant Signal Behav. – 2008. – Vol. 3. – P.156-165.
8. Suzuki N, Mittler R. Reactive oxygen species and temperature stresses: A delicate balance between signaling and destruction // Physiol. Plant. – 2006. – Vol.. 126. – P. 45-51.
9. Walker-Simmons M., Kudrna D.A., Warner RL. Reduced accumulation of ABA during water stress in a molybdenum cofactor mutant of barley // Plant Physiol. –1988. –Vol. 90. –P. 728-733
10. KoshibaT., SaitoE., OnoN., YamamotoN., SatoM. Purification and properties of flavin and molybdenum-containing aldehyde oxidase from coleoptiles of maize // Plant Physiol. –1996. – Vol.110. –P.781-789.
11. Beauchamp C., Fridovich J. Superoxide Dismutase: Improved Assays and an Assay Applicable to Acrylamide Gels // Anal. Biochem. –1971.–Vol. 44. –P. 276-287.
12. Лебедева О.В., Угарова Н.Н., Березин И.В. Кинетическое изучение реакции окисления о-дианизидина Н2О2 в присутствии пероксидазы хрена // Биохимия. –1977.–Т.42. – С.1372-1379.
13. Rothe G.M. Aldehyde oxidase isoenzymes (EC 1.2.3.1) in potato tubers (Solanumtuberosum). //Plant Cell Physiol. –1974.–Vol.15.–Р.493-499.
14. Laemmli K. Cleavage of structural proteins during the assembly of the headof bacteriophage // Nature. –1970. –Vol.4. – №227. –P.680-685.
15. Oliver H. Lowry, Nira J. Rosebrough, A.Lewis Farr and Rose J. Randall Protein measurement with the folin phenol reagent // J. Biol. Chem. –1951. –Vol.193. – P. 265-275.
References
1. Tardieu F. Plant tolerance to water deficit: physical limits and possibilities for progress // Comp. Rend. Geosci. –2005. –Vol. 337.–P. 57-67.
2. Fehr W.R., Caviness C.E., Burmood O.T. and Pennington J.S. Stage of development description for soybeans Glycine max(L.) // Merril. Crop Sci. – Vol.11. – P. 929-931.
3. Chaves M.M., Oliveira M.M. Mechanisms underlying plant resilience to water deficits: prospects for water-saving agriculture // J.Exp. Bot. –2004. –V. 55. –No.55. –P.2365-2384.
4. Kolupaev Y.E., Karpets Y.V. Formation of adaptive responses of plants to abiotic stressors action. –Kiev: Osnova, 2010. – 351 p.
5. Maevskaya S.N., Nikolaeva M.K. Response of Antioxidant and Osmoprotective Systems of Wheat Seedlings to Drought and Rehydration. // Russian Journal of Plant Physiology. – 2013.–V. 60. – No.3. –Р.351–359.
6. Varga B., Janda T., La´szlo´ E., Veisz O. Influence of abiotic stresses on the antioxidant enzyme activity of cereals. // ActaPhysiol Plant. –2012.–Vol.34. –Р.849–858.
7. Helena M. Carvalho C. Drought stress and reactive oxygen species. Production, scavenging and signaling // Plant Signal Behav. – 2008. – Vol. 3. – P.156-165.
8. Suzuki N, Mittler R. Reactive oxygen species and temperature stresses: A delicate balance between signaling and destruction // Physiol. Plant. – 2006. – Vol. 126. – P. 45-51.
9. Walker-Simmons M., Kudrna D.A., Warner RL. Reduced accumulation of ABA during water stress in a molybdenum cofactor mutant of barley // Plant Physiol. –1988. – Vol. 90. –P. 728-733
10. KoshibaT., SaitoE., OnoN., YamamotoN., SatoM. Purification and properties of flavin and molybdenum-containing aldehyde oxidase from coleoptiles of maize // Plant Physiol. –1996. – Vol.110. –P.781-789.
11. Beauchamp C., Fridovich J. Superoxide Dismutase: Improved Assays and an Assay Applicable to Acrylamide Gels // Anal. Biochem. –1971.–Vol. 44. –P. 276-287.
12. Lebedev O.V., Ugarov N.N., Berezin I.V. Kinetic study of the oxidation reaction of o-dianisidine in the presence of H2O2 horseradish peroxidase // Biochemistry. – 1977. – Vol.42.– P.1372-1379.
13. Rothe G.M. Aldehyde oxidase isoenzymes (EC 1.2.3.1) in potato tubers (Solanumtuberosum). //Plant Cell Physiol. –1974.–Vol.15.–Р.493-499.
14. Laemmli K. Cleavage of structural proteins during the assembly of the headof bacteriophage // Nature. –1970. –Vol..4. – №227. –P.680-685.
15. Oliver H. Lowry, Nira J. Rosebrough, A.Lewis Farr and Rose J. Randall Protein measurement with the folin phenol reagent // J. Biol. Chem. –1951. –Vol.193. – P. 265-275.
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ФИЗИОЛОГИЯ И БИОХИМИЯ РАСТЕНИЙ
