Abstract
The activity of a range of endo- and exopeptidase enzymes have been measured in the glumes, flag leaf and stem during the period of grain development in wheat. The enzymes show a sequential pattern of appearance with activity peaks occurring at a number of intervals from anthesis until just prior to the cessation of grain growth. Of the enzymes studied only the haemoglobin- and casein-degrading activity and alanylglycine-dipeptidase activity increased during the period of rapid protein loss, while aminopeptidase, carboxypeptidase and leucyltyrosine dipeptidase reached maximum activity prior to this period.
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References
Arnon, D.I.: Copper enzymes in isolated chloroplasts, polyphenol oxidase inBeta vulgaris. Plant Physiol.24, 1–15 (1949)
Collier, M.D., Murray, D.R.: Leucyl-β-naphthylamidase activities in developing seeds and seedlings ofPisum sativum L. Aust. J. Plant Physiol.4, 571–582 (1977)
Dalling, M.J., Boland, G., Wilson, J.H.: Relation between acid proteinase activity and redistribution of nitrogen during grain development in wheat. Aust. J. Plant Physiol.3, 721–730 (1976)
Feller, U.: Changes in nitrogen contents and in proteolytic activities in different parts of field grown wheat ears (Triticum aestivum L.) during maturation. Plant Cell Physiol.19, 1489–1495 (1978)
Feller, U.K., Soong, T-S.T., Hageman, R.H.: Leaf proteolytic activities and senescence during grain development of field grown corn (Zea mays L.). Plant Physiol.59, 290–294 (1977)
Frith, G.J.T., Bruce, D.G., Dalling, M.J.: Distribution of acid proteinase activity in wheat seedlings. Plant Cell Physiol.16, 1085–1091 (1975)
Frith, G.J.T., Gordon, K.H.J., Dalling, M.J.: Proteolytic enzymes in green wheat leaves. I. Isolation on DEAE-cellulose of several proteinases with acid pH optima. Plant Cell Physiol.19, 491–500 (1978a)
Frith, G.J.T., Swinden, L.B., Dalling, J.J.: Proteolytic enzymes in green wheat leaves. II. Purification by affinity chromatography, and some properties of proteinases with acid pH optima. Plant Cell Physiol.19, 1029–1041 (1978b)
Lowry, O.H., Rosebrough, M.J., Farr, A.L., Randall, R.J.: Protein measurement with Folin phenol reagent. J. Biol. Chem.193, 265–275 (1951)
Mikola, J., Kolehmainen, L.: Localization and activity of various peptidases in germinating barley. Planta104, 167–177 (1972)
Nair, T.V.R., Grover, H.L., Abrol, Y.P.: Nitrogen metabolism of the upper three leaf blades of wheat at different soil nitrogen levels. II. Protease activity and mobilization of reduced nitrogen to the developing grains. Physiol. Plant.42, 293–300 (1978)
Peoples, M.B., Dalling, M.J.: Degradation of ribulose 1,5-bisphosphate carboxylase by proteolytic enzymes from crude extracts of wheat leaves. Planta138, 153–160 (1978)
Ryan, C.A.: Proteolytic enzymes and their inhibitors in plants. Annu. Rev. Plant Physiol.24, 173–196 (1973)
Salmia, M.A., Mikola, J.J.: Activities of two peptidases in resting and germinating seeds of Scots pine,Pinus sylvestris. Physiol. Plant.33, 261–265 (1975)
Sofield, I., Evans, L.T., Wardlaw, I.F.: The effects of temperature and light on grain filling in wheat. In: Mechanisms of Regulation of Plant Growth, pp. 909–915, Bieleski, R.L., Ferguson, A.R., Creswell, M.M., eds. Bull. 12, Roy. Soc. N.Z., Wellington 1974
Sopanen, T., Carfantan, N.: Activities of various peptidases in the senescing petals of tulips. Physiol. Plant.36, 247–250 (1976)
Waters, S.P., Dalling, M.J.: Distribution and characteristics of aminoacyl β-naphthylamidase activities in wheat seedlings. Aust. J. Plant Physiol.6, 595–606 (1979)
Wittenbach, V.A.: Breakdown of ribulose bisphosphate carboxylase and change in proteolytic activity during dark-induced senescence of wheat seedlings. Plant Physiol.62, 604–608 (1978)
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Waters, S.P., Peoples, M.B., Simpson, R.J. et al. Nitrogen redistribution during grain growth in wheat (Triticum aestivum L.). Planta 148, 422–428 (1980). https://doi.org/10.1007/BF00552654
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DOI: https://doi.org/10.1007/BF00552654