Abstract
Hydrolysis of 13S globulin, the main storage protein in grains of common buckwheat (Fagopyrum esculentum Moench), proceeds in at least two phases during germination. The first stage, involving a limited proteolytic cleavage of the protein, is associated with increased activity of proteases having maximum activity at pH 7.6. The second stage, involving further hydrolysis of the partially cleaved protein, starts after 12 h of imbibition. During this phase, activity of proteases increased and activity maximum shifted to pH 5.6. Nevertheless, 13S globulin retains its antigenic identity till the emergence of radicle and plumule. Thus, it may not be the major source of amino acids utilized by the germinating seed during the initial stages of imbibition.
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References
Benyon, R.J., Bond, J.S. (ed.): Proteolytic Enzymes: A Practical Approach.-IRL Press, Oxford 1989.
Bewley, J.D., Black, M.: Physiology and Biochemistry of Seeds in Relation to Germination. Vol. I. Development, Germination and Growth.-Springer-Verlag, Berlin 1978.
Bewley, J.D., Black, M.: Physiology of Development and Germination.-Plenum Press, New York 1985.
Bradford, M.A.: A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of dye binding.-Anal. Biochem. 72: 248–254, 1976.
Bryant, J.L., Hosangadi, P., Beachy, R.N.: The β-conglycinins of soyabean remain assembled in a 7S conformation while undergoing proteolytic cleavage during germination and early seedling growth.-Plant Cell Physiol. 36: 1059–1065, 1995.
Callis, J.: Regulation of protein degradation.-Plant Cell 7: 845–857, 1995.
Dunaevsky, Y.E., Belozersky, M.A.: Proteolysis of the main storage protein of buckwheat seeds at early stages of germination.-Physiol. Plant. 75: 424–428, 1989.
Elpidina, E.N., Voskoboynikova, N.E., Belozersky, M.A., Dunaevsky, Y.E.: Localization of metalloproteinase and its inhibitor in the protein bodies of buckwheat seeds.-Planta 185: 46–52, 1991.
Fincher, G.B.: Molecular and cellular biology associated with endosperm utilization in germinating cereal grains.-Annu. Rev. Plant Physiol. Plant mol. Biol. 40: 305–346, 1989.
Hara, I., Matsuhara, H.: Pumpkin (Cucurbita sp.) seed globulin V. Proteolytic activities involved in globulin degradation in ungerminating seeds.-Plant Cell Physiol. 21: 219–232, 1980a.
Hara, I., Matsuhara, H.: Pumpkin (Cucurbita sp.) seed globulin VI. Proteolytic activities appearing in germinating cotyledons.-Plant Cell Physiol. 21: 233–245, 1980b.
Hara, I., Wada, K., Matsuhara, H.: Pumpkin (Cucurbita sp.) seed globulin II. Alterations during germination.-Plant Cell Physiol. 17: 815–823, 1976.
Harlow, E., Lane, D.: Antibodies: a Laboratory Manual.-Cold Spring Harbor Laboratory Press, Cold Spring Harbor 1988.
Hudson, L., Hay, F.C.: Practical Immunology.-Blackwell, London 1989.
Kamata, Y., Fukuda, M., Sone, H., Yamauchi, F.: Relationship between limited proteolysis of glycinin and its conformation.-Agr. biol. Chem. 55: 149–155, 1991.
Rosen, M.K.: A modified ninhydrin colorimetric method for analysis of amino acids.-Arch. Biochem. Biophys. 67: 10–15, 1957.
Rout, M.K., Chrungoo, N.K.: Partial characterization of the lysine rich 13S globulin from buckwheat (Fagopyrum esculentum Moench): Its antigenic homology with seed proteins of other crops.-Biochem. mol. Biol. int. 40: 587–595, 1996.
Shutov, A.D., Vaintraub, I.A.: Degradation of storage proteins in germinating seeds.-Phytochemistry 26: 1557–1566, 1987.
Towbin, H., Stachelin, T., Gordon, J.: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications.-Proc. nat. Acad. Sci. USA 76: 4350–4354, 1979.
Vierstra, R.D.: Proteolysis in plants: mechanisms and functions.-Plant mol. Biol. 32: 275–302, 1993.
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Rout, M., Chrungoo, N. Mobilization of Reserve Proteins During Early Stages of Seed Germination in Fagopyrum Esculentum. Biologia Plantarum 42, 81–87 (1999). https://doi.org/10.1023/A:1002123627361
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DOI: https://doi.org/10.1023/A:1002123627361