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Amylase activity and growth in internodes of deepwater rice

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Abstract

Isoelectrofocusing, product analysis, thermal denaturation studies and affinity chromatography on cycloheptaamylose-Sephadex were used to identify the amylolytic enzymes in internodes of deepwater rice (Oryza sativa L.). Amylolytic activity in internodes of deepwater rice consists of α-amylase (sometimes separated into two isoforms) and of β-amylase. During submergence of whole plants, α-amylase activity increases in young, growing internodes, but β-amylase activity declines. Although non-growing, mature internodes contain higher levels of β-amylase than do the elongating younger internodes, the effect of submergence on amylase activities in both tissues follows the same trend. Submergence, gibberellic acid (GA3) and ethylene all promote α-amylase activity in growing and non-growing internodes of excised deepwater-rice stem sections. Inhibitor studies showed that submergence and ethylene promote α-amylase activity in the absence of endogenous gibberellin (GA), and GA3 enhances α-amylase activity when ethylene action is inhibited. Therefore, ethylene and GA appear to increase α-amylase activity independently of each other. Enhanced α-amylase activities are probably responsible for the mobilization of carbohydrates which are needed to support internode elongation during submergence of deepwater rice.

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Abbreviations

CHA:

cycloheptaamylose

GA3 :

gibberellic acid

NBD:

2,5-norbornadiene

TCY:

tetcyclacis

References

  • Bernfeld, P. (1955) Amylases, α and β. Methods Enzymol. 1, 149–158

    Google Scholar 

  • Bleecker, A.B., Schuette, J.L., Kende, H. (1986) Anatomical analysis of growth and developmental patterns in the internode of deepwater rice. Planta 169, 490–497

    Google Scholar 

  • Carter, J.L., Garrard, L.A., West, S.H. (1973) Effect of gibberellic acid on starch degrading enzymes in leaves of Digitaria decumbens. Phytochemistry 12, 251–254

    Google Scholar 

  • Chrispeels, M.J., Varner, J.E. (1967) Gibberellic acid-enhanced synthesis and release of α-amylase and ribonuclease by isolated barley aleurone layers. Plant Physiol 42, 398–406

    Google Scholar 

  • Cohen, E., Kende, H. (1986) The effect of submergence, ethylene and gibberellin on polyamines and their biosynthetic enzymes in deepwater-rice internodes. Planta 169, 498–504

    Google Scholar 

  • Cohen, E., Kende H. (1987) In vivo 1-aminocyclopropane-1-carboxylate synthase activity in internodes of deepwater rice: Enhancement by submergence and low oxygen levels. Plant Physiol. (in press)

  • Dunn, G. (1974) A model for starch breakdown in higher plants. Phytochemistry 14, 1341–1346

    Google Scholar 

  • Eastwell, K.C., Spencer, M.S. (1982a) Effect of ethylene on the gibberellic acid enhanced synthesis and release of amylase by isolated barley aleurone layers. Plant Physiol. 69, 557–562

    Google Scholar 

  • Eastwell, K.C., Spencer, M.S. (1982b) Modes of ethylene action in the release of amylase from barley aleurone layers. Plant Physiol. 69, 563–567

    Google Scholar 

  • Greenwood, C.T., MacGregor, A.W. (1965) The isolation of α-amylase from barley and malted barley, and a study of the properties and action-patterns of the enzymes. J. Inst. Brewing 71, 405–417

    Google Scholar 

  • Ho, T.-H.D., Abroms, J., Varner, J.E. (1982) Effect of ethylene on the release of α-amylase through cell walls of barley aleurone layers. Plant Physiol. 69, 1128–1131

    Google Scholar 

  • Jacobsen, J.V. (1973) Interactions between gibberellic acid, ethylene and abscisic acid in control of amylase synthesis in barley aleurone layers. Plant Physiol. 51, 198–202

    Google Scholar 

  • Jacobsen, J.V. (1983) Regulation of protein synthesis in aleurone cells by gibberellin and abscisic acid. In: The biochemistry and physiology of gibberellins, vol. 2, pp. 159–187, Crozier, A., ed. Praeger, New York

    Google Scholar 

  • Jacobsen, J.V., Hanson, A.D., Chandler, P.C. (1986) Water stress enhances expression of an α-amylase gene in barley leaves. Plant Physiol. 80, 350–359

    Google Scholar 

  • Jones, R.L. (1968) Ethylene enhanced release of α-amylase from barley aleurone cells. Plant Physiol. 43, 442–444

    Google Scholar 

  • Katsumi, M., Fukuhara, M. (1969) The activity of α-amylase in the shoot and its relation to gibberellin-induced elongation. Physiol. Plant. 22, 68–75

    Google Scholar 

  • McComb, A.J., Broughton, W.J. (1971) Metabolic changes in internodes of dwarf pea plants treated with gibberellic acid. In: Plant growth substances 1970, pp. 407–413, Carr, D.J., ed. Springer-Verlag, New York

    Google Scholar 

  • Métraux, J.-P., Kende, H. (1983) The role of ethylene in the growth response of submerged deep water rice. Plant Physiol. 72, 441–446

    Google Scholar 

  • Miyata, S., Okamoto, K., Watanabe, A., Akazawa, T. (1981) Enzymic mechanism of starch breakdown in germinating rice seeds. In vivo and in vitro synthesis of α-amylase in rice seed scutellum. Plant Physiol. 68, 1314–1318

    Google Scholar 

  • Nitta, Y., Mizushima, M., Hiromi, K., Ono, S. (1971) Influence of molecular structures of substrates and analogues on takaamylase A catalyzed hydrolyses. I. Effect of chain length of linear substrates. J. Biochem. 69, 567–576

    Google Scholar 

  • Palmiano, E.P., Juliano, B.O. (1972) Biochemical changes in the rice grain during germination. Plant Physiol. 49, 751–756

    Google Scholar 

  • Perez, C.M., Palmiano, E.P., Baun, L.C., Juliano, B.O. (1971) Starch metabolism in the leaf sheaths and culm of rice. Plant Physiol 47, 404–408

    Google Scholar 

  • Raskin, I., Kende, H. (1984a) Regulation of growth in stem sections of deep-water rice. Planta 160, 66–72

    Google Scholar 

  • Raskin, I., Kende, H. (1984b) Role of gibberellin in the growth response of submerged deep water rice. Plant Physiol. 76, 947–950

    Google Scholar 

  • Raskin, I., Kende, H. (1984c) Effect of submergence on translocation, starch content and amylolytic activity in deep-water rice. Planta 162, 556–559

    Google Scholar 

  • Silvanovich, M.P., Hill, R.D. (1976) Affinity chromatography of cereal α-amylases. Anal. Biochem. 73, 430–433

    Google Scholar 

  • Tanaka, Y., Ito, T., Akazawa, T. (1970) Enzymic mechanism of starch breakdown in germinating rice seeds. III. α-Amylase isozymes. Plant Physiol. 46, 650–654

    Google Scholar 

  • Vergara, B.S., Jackson, B., DeDatta, S.K. (1976) Deep-water rice and its response to deep-water stress. In: Climate and rice, pp. 301–319 International Rice Research Institute, Los Baños, Philippines

    Google Scholar 

  • Vretblad, P. (1974) Immobilization of ligands for biospecific affinity chromatography via their hydroxyl groups. The cyclohexaamylose-β-amylase system. FEBS Lett. 47, 86–89

    Google Scholar 

  • Weselake, R.J., Hill, R.D. (1982) Cycloheptaamylose as an affinity ligand of cereal alpha amylase. Characteristics and a possible mechanism of the interaction. Carbohydrate Res. 108, 153–161

    Google Scholar 

  • Würsch, P., Roulet Ph. (1982) Quantitative estimation of maltooligosaccharides by high-performance thin-layer chromatography. J. Chromatog. 244, 177–182

    Google Scholar 

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Smith, M.A., Jacobsen, J.V. & Kende, H. Amylase activity and growth in internodes of deepwater rice. Planta 172, 114–120 (1987). https://doi.org/10.1007/BF00403036

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  • DOI: https://doi.org/10.1007/BF00403036

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