Tevrican DOKUYUCU, Ziya DUMLUPINAR, Aydın AKKAYA

Identification of Turkish oat landraces (Avena sativa L.) based on avenin proteins by sds-page Technique

Oat genotypes exhibit valuable and reproducible polymorphism in the avenin pattern which is important to identify genotypes and to use in breeding programs. Therefore, in this study, 196 Turkish oat landraces (Avena sativa L.) and three commercial cultivars (Checota, Faikbey and Seydisehir) were identified using the SDS-PAGE technique based on oat avenin protein band numbers and molecular weights. Results indicate that genotypes varied in avenin protein band numbers and molecular weights. Avenin protein band numbers and molecular weights ranged from 4 to 16, and 8.8 to 45 kDa, respectively. The bands having the highest molecular weight (45 kDA) was obtained from E19 and E45 genotypes, while the bands having the lowest molecular weights were obtained from A76, A81, A79, E20 and A29 genotypes (8.8, 9.2, 9.5, 9.6 and 9.8 kDa, respectively). A18, A34 and K3 genotypes had the lowest avenin bands (4), while E20 and A54 genotypes had the highest avenin bands (15 and 16, respectively).According to genetic similarity analysis based on avenin protein band numbers and molecular weights, oat genotypes clustered in two major groups at 0.240 genetic similarities. The first major group consisted of A53, E37, E59, A23, A34, and A41 genotypes. In this group, A23-A41 and A53-E37 genotypes were similar with 0.801 and 0.767 coefficients respectively. The second group consisted of three large groups and several small groups. The genotypes clustered in many groups with a large number of genetic similarity coefficients. A2-E57 and K13-K35 genotypes were the most similar with 0.920 genetic similarity coefficients.

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Ahokas, H., M.L. Manninen, 2000. Retrospecting genetic variation of Finnish oat (Avena sativa L.) landraces and observation on revived lines grown prior to 1957. Genetic Resources and Crop Evolution. 47:345-352.
Ahokas, H., E. Heikkila, M.L. Alho, 2005. Variation of oat (Avena) protein fractions of interest in celiac grain diets. Genetic Resources and Crop Evolution. 52:813-819.
Baum, B.R. 1977. Oats: Wild and Cultivated. Can. Dep. Agric, Ottawa Ontario.
Bewley, J.D., M. Black, 1994. Seeds: Physiology of Development and Germination. Plenum Press. New York.
Chesnut, R.S., M.A. Shotwell, S.K. Boyer, B.A. Larkins, 1989. Analysis of avenin proteins and the expression of their mRNAs in developing oat seeds. The Plant Cell. 1:913-924.
Clark, D., 2005. Proteomics: The Global Analysis of Proteins. In: Molecular Biology. Elsevier Academic Press. ISBN: 0-12- 175551-7, pp 717-744.
Dice, L.R., 1945. Measures of the amount of ecologic association between species. Ecology. 26:297-302.
Dumlupınar, Z., 2010. Türkiye Orijinli Yerel Yulaf Genotiplerinin Avenin Proteinleri ile Morfolojik, Fenolojik ve Agronomik Özellikler Yönünden Karakterizasyonu. KSÜ Fen Bilimleri Enstitüsü Tarla Bitkileri Anabilim Dalı, Doktora Tezi, 112 s. (http://kutuphane.ksu.edu.tr/etez/ fbe/T01357/Ziya_DUMLUPINAR_Tez.pdf)
Dvoracek, V., V. Curn, J. Moudry, 2003. Suitability of oat-seed storage protein markers in grain and mixed flour samples. Plant Soil Environ. 49(11):486-491.
Frey, K.J. 1951. The relation between alcohol-soluble and total nitrogen contents of oats. Cereal Chem. 28:506-509.
Gevaert, K., J. Vandekerckhove, 2000. Protein identification methods in proteomics. Electrophoresis. 21:1145-1154.
Hansen, A.E., A. Nassuth, I. Altosaar, 1988. Rapid electrophoresis of oat (A. sativa L.) prolamines from single seeds for cultivar identification. Cereal Chem. 65(2):152-154.
Jussila, M., T. Sontag-Strohm, O. Ulvinen, 1992. The identification of Finnish oat cultivars (Avena sativa L.) by the use of SDSPAGE of the avenins in homogeneous and gradient. Acta Agriculturae Scandinavica, Section B- plant Science. 42(2): 106-110.
Kim, S.I., L. Charbonnier, J. Mosse, 1978. Heterogeneity of avenin, the oat prolamin. Fractionation, molecular weight and amino acid composition. Biochim. Biophys. Acta. 537(1):22-30.
Larsen, M.R., P. Roepstorff, 2000. Mass spectrometric identification of proteins and characterization of their posttranslational modifications in proteome analysis. Fresenius J. Anal. Chem. 366:677-690.
Leammli, U.K. 1970. Cleavage of structural proteins assembly of the head of bacteriophage T4. Nature. 227:680-685.
Leisova, L., L. Kucera, L. Dotlacil, 2007. Genetic resources of barley and oat characterised by microsatellites. Czech Journal of Genetics and Plant Breeding. 43(3):97-104.
Lookhart, G.L. 1985. Identification of oat cultivars by combining polyacrylamide gel electrophoresis and reversed-phased highperformance liquid chromatography. Cereal Chem 62(5): 345- 350.
Luthe, D.S. 1987. Storage protein synthesis during oat (Avena sativa L.) seed development. Plant Physiol. 84:337-340.
Mirza, B., M. Shoaib, M. Ahmad Y.B. Fu, 2007. Genetic diversity in Pakistani population of Avena fatua revealed by seed storage protein polymorphism. Communications in Biometry and Crop Science. 2(1):41-48.
Mosse, J. 1966. Alcohol-soluble proteins of cereal grains. In: Fed. Proc. Amer. Soc. Exp. Biol. Fed. pp 1663-1669.
Örçen, N., G. Bilgen, I. Demir, D.W. De Joung, 1995. Yulaf (Avena sativa L.) depo proteininin (prolamin) elektroforeziyle çesit tanımı. Tarla Bitkileri Bilimi Derneği, E. Ü. Z. F. Tarla Bitkileri Bölümü, TÜBİTAK-MAM, İ. Ü. BİYOGEM ve TÜBİTAK. Workshop “Biyoteknoloji ve Bitki Islahı” 17-19 Nisan 1995. Gebze- Kocaeli, pp 72-77.
Portyanko, V.A., N.R. Sharopova, A.A. Sozinov, 1998. Characterisation of European oat germplasm: allelic variations at complex avenin loci detected by acid polyacrylamide gel electrophoresis. Euphytica. 102:15-27.
Pernollet, J.C., S.I. Kim, J. Mosse, 1982. Characterization of storage proteins extracted from Avena sativa seed protein bodies. J. Agric. Food Chem. 30:32-36.
Peterson, D.M., D. Smith, 1976. Changes in nitrogen and carbohydrate fractions in developing oat groats. Crop Sci. 16:67-71.
Peterson, D.M., R.H. Saigo, J. Holy, 1988. Oat cultivar identification by electrophoresis of seed proteins. Third Int. Oat Conf. Proc., Lund, Sweden, 4-8 July, pp. 371.
Robert, L.S., A. Cudjoe, C. Nozzolillo, I. Altosaar, 1983. Total solubilization of storage protein in oat (Avena sativa L. cv. Hinoat): evidence that glutelins are a minor component. J. Can. Inst. Food Sci. Technol. 16:196-200.
Rohlf, F.J., 2005. NTSYS-pc: Numerical Taxonomy and Multivariate Analysis System Version 2.2. Setauket, Exeter Publishing, New York.
Yano, H., J.H. Wong, Y.M. Lee, M.J. Cho, B.B. Buchanan, 1998. A strategy for the identification of proteins targeted by thioredoxin. PNAS. 98(8): 4794-4799.