Influence of a low-temperature stress on amino acid structure of wheat isoperoxidases
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Keywords:
amino acid structure, isoperoxidases, water repellency (hydrophobicity), cluster analysis, lowtemperature stress, wheatAbstract
Under the influence of a low-temperature stress changes of amino acid structure of the cathode isoperoxidases A25 and A32 from seedlings of various frost resistance wheat were observed. Three groups of the amino acids are revealed, which content increases, decreases and varies slightly under the low-temperature conditions. Changes of average water repellency (hydrophobicity) of amino acid structure of isoperoxidases, also the content of histidine, lysine, arginine, alanine, serine at the low-temperature action are obtained. In the correlation analysis entering the clustering program, high coefficients of correlation between separate amino acids are established. The received results testify in favor of modifications of activity and isoenzyme structure of the peroxidases necessary for reorganization of plant metabolic processes in the temperature stress conditionsReferences
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2. Cansev A., Gulen H., Eris A. The activities of catalase and peroxidase in olive (Olea europaca L.cv.Gemlik) under low temperature stress // Horticulture, Environment and Biotechnology,2011.-V.52.-N2.-P.113-120.
3. Савич И.М. Изопероксидазный состав проростков кукурузы как тест на холодоустойчивость// Сельскохозяйственная биология. – 1987. - № 5. – С.65-69.
4. Перуанский Ю.В., Тажибаева Т.Л., Абугалиева А.И. Способ определения устойчивости генотипов пшеницы к стрессовым факторам.- Патент Республики Казахстан № 23504, 1999.
5. Тажибаева Т.Л. Рекомендации по применению нового прижизненного метода оценки морозостойкости пшеницы в селекционной практике.- Алматы: КПР МСХ, 1995. - 18 с.
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7. Kohler G.O., Palter R. Studies on methods for amino acid analysis of wheat products// Cereal Chem. - 1967. - V.44. - N 5. - P. 512-521.
8. Bigelow C.C. The average water repellency( hydrophobicity) of proteins and the relation between it and protein structure// J.Theoret. Biol. - 1967. - V.16. - N 2. - P.187-211.
9. Lawson E. Q., Sadler A. J., Harmatz D., E.A. A simple experimental model for hydrophobic interactions in proteins// J.Biol.Chem. - 1984. - V.259. - N 5. - Р.2910-2912.
10. Бергер В.Я. и Подлипаева Ю.И. Cтрессорные белки и соленость внешней среды.// Труды Зоологического института РАН , 2013. – Прил. № . –С. 22–32.
11. Miao Y., Lv D., Wang P., Wang X.C., Chen J., Miao C., Song C.P. An Arabidopsis glutathione peroxidase functions as both a redox transducer and a scavenger in abscisic acid and drought stress responses. // Plant Cell, 2006. – V. 18. -P. 2749–2766.
12. Haluskova L., Valentovicova K., Huttova J., Mistrık I., Tamas L. Effect of abiotic stresses on glutathione peroxidase and glutathione S-transferase activity in barley root tips .//Plant Physiology and Biochemistry , 2009/ -V.47 . –P.1069–1074.
13. Milla M.A.R., Maurer A., Huete A.R., Gustafson J.P. Glutathione peroxidase genes in Arabidopsis are ubiquitous and regulated by abiotic stresses through diverse signalling pathways. // Plant J., 2003 – V.36 . - P. 602–615.
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Tazhibayeva, T. L. (2015). Influence of a low-temperature stress on amino acid structure of wheat isoperoxidases. Experimental Biology, 60(2), 410–413. Retrieved from https://bb.kaznu.kz/index.php/biology/article/view/987
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