Abstract
Two inbred lines of rye (Secale cereale L), the kernels of which displayed a very low level of β-amylase activity (1–3% of the levels generally found in rye), were investigated in comparison with a third normal line. An anti-wheat β-amylase immune serum which cross-reacted with the rye enzyme was used in this study.
The anti-wheat β-amylase immune serum absorbed the β-amylase activity in the three lines which were investigated. Comparably small amounts of enzymatic antigen corresponded to the small levels of activity detected in the enzyme-deficient lines. The three inbred lines were equally able to germinate. One of the enzyme-deficient lines was further investigated and neither the level of activity nor the amount of enzymatic antigen were notably changed upon germination.
The results indicate that the reduced activity is due neither to the presence of an inhibitor nor to the production of inactive enzymes. Germination can proceed normally without late production of β-amylase.
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References
Burnett, K.G., Helder, M.R. (1978) Peromyscus alcohol dehydrogenase: lack of cross reacting material in enzyme negative animals. Biochem. Genet. 16, 1093–1105
Clarke, H.G.M., Freeman, T. (1967) A quantitative immunoelectrophoresis method. In: Protides of the biological fluids, vol. XIV, pp. 503–509, Peeters H., ed. Elsevier, Amsterdam
Chojnacki, G., Bryklzynski, J., Tymieniecka, E. (1976) Preliminary information on sprouting in Triticale. Cereal Res. Comm. 4, 111–114
Daussant, J. (1977) Immunochemical approach to questions related to α and β-amylases in barley and wheat. In: Enzymes in food and beverage processing, Amer. Chem. Soc. Symp. Ser. No. 47, pp. 80–99
Daussant, J. (1978) Caractérisation immunochimique d' α-amylases de grain de Blé à différents stades ontogéniques. Ann. Immunol. (Inst. Pasteur) 129L, 215–232
Daussant, J., Hill, R.D. (1979) Immunochemical identification of α-amylases in developing, mature and germinated Triticale seeds. Physiol. Plant. 45, 255–259
Daussant, J., Laurière, C., Carfantan, N., Skakoun, A. (1977) Immunochemical approaches to questions concerning enzyme regulation in plants. In: Regulation of enzyme synthesis and activity in higher plants, pp. 197–223, Smith, H. ed. Academic Press, London New York San Francisco
Harris, G. (1962) The enzyme content and enzymatic transformation of malt. In: Barley and malt, pp. 583–694, Cook, A.H., ed. Academic Press, New York London
Krøll, J. (1973) Rocket-line immunoelectrophoresis. Scand. J. Immunol. 2, Suppl. 1, 85–87
Nummi, M., Daussant, J., Niku-Paavola, M.L., Kalsta, M., Enari, J.M. (1970) Comparative immunological and chromatographic study of some plant β-amylases. J. Sci. Food Agric. 21, 258–260
Okamoto, K., Akazawa, T. (1980) Enzymic mechanism of starch breakdown in germinating rice seeds, de novo synthesis of β-amylase. Plant Physiol. 65, 81–84
Ouchterlony, O. (1949) Antigen — antibodies reactions in gels. Acta Pathol. Microbiol. Scand. 26, 507–515
Rowsell, E.V., Goad, L. (1962) The constituents of wheat binding latent β-amylase. Biochem. J. 84, 73
Scandalios, J.G. (1974) Isoenzymes in development and differentiation. Annu. Rev. Plant Physiol. 25, 225–258
Spizek, J., Janecek, J. (1969) The effect of ethionine on the synthesis of β-Galactosidase: formation of an immunologically cross reacting protein. Biochem. Biophys. Res. Commun. 34, 17–21
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Daussant, J., Zbaszyniak, B., Sadowski, J. et al. Cereal β-amylase: Immunochemical study on two enzyme-deficient inbred lines of rye. Planta 151, 176–179 (1981). https://doi.org/10.1007/BF00387820
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DOI: https://doi.org/10.1007/BF00387820