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Trypsin inhibitors in Pisum: variation in amount and pattern of accumulation in developing seed

  • C. Domoney (a1) and T. Welham (a1)
Abstract

A survey of Pisum genotypes for seed trypsin inhibitors revealed a tenfold range in the extent of inhibition. Approximately 90% of trypsin inhibitory activity was associated with two albumin fractions in selected variant lines. The differences among extreme variants were consistent in three environments, between two sources of trypsin tested and whether expressed on a unit protein or dry weight basis.

A study of the appearance of trypsin inhibitors during seed development in selected highand low-inhibitor lines showed differences in the accumulation pattern of active inhibitors. An endogenous protease was identified in Pisum seed protein preparations, whose in vitro trypsin-like activity was predominant in protein from early stages of seed development, when little or no trypsin inhibitor was present. However, there was no correlation between the amount of this protease and the extent of trypsin inhibitory activity in lines that varied for inhibitor content.

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COPYRIGHT: © Cambridge University Press 1992
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References
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Adams, C.A. and Rinne, R.W. (1981) The occurrence and significance of dispensable proteins in plants. New Phytologist 89, 1–14.
Arthur, A.E., Adams, H., Strouts, K., Jones, D.A., Wang, T.L. and Hedley, C.L. (1991) An analysis of seed development in Pisum sativum. XV. The influence of seed size on protein content. Seed Science Research 1, 203–208.
Barratt, D.H.P. and Clark, J.A. (1991) Proteins arising during the late stages of embryogenesis in Pisum sativum L. Planta 184, 14–23.
Barratt, D.H.P., Domoney, C. and Wang, T.L. (1989) Purification and partial characterisation of two abscisic acid-responsive proteins induced in cultured embryos of Pisum sativum L. Planta 180, 16–23.
Bjerg, B., Eggum, B.O. and Sorensen, H. (1989) Antinutritional factors in pea and faba beans. pp. 351–358 in Huisman, J., van der Poel, T.F.B. and Liener, I.E. (Eds) Recent advances of research in antinutritional factors in legume seeds. Wageningen PUDOC.
Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248–254.
Brown, W.E., Takio, K., Titani, K. and Ryan, C.A. (1985) Wound-induced trypsin inhibitor in alfalfa leaves: identity as a member of the Bowman-Birk inhibitor family. Biochemistry 24, 2105–2108.
Close, T.J., Kortt, A.A. and Chandler, P.M. (1989) A cDNA-based comparison of dehydration-induced proteins (dehydrins) in barley and corn. Plant Molecular Biology 13, 95–108.
Dure, L. III, Crouch, M.L., Harada, J., Ho, T-H.D., Mundy, J., Quatrano, R., Thomas, T. and Sung, Z.R. (1989) Common amino acid sequence domains among the LEA proteins of higher plants. Plant Molecular Biology 12, 475–486.
Graham, J.S., Pearce, G., Merryweather, J., Titani, K., Ericsson, L. and Ryan, C.A. (1985a) Wound-induced proteinase inhibitors from tomato leaves. I. The cDNA-deduced primary structure of pre-inhibitor I and its post-translational processing. Journal of Biological Chemistry 260, 6555–6560.
Graham, J.S., Pearce, G., Merryweather, J., Titani, K., Ericsson, L.H. and Ryan, C.A. (1985b) Wound-induced proteinase inhibitors from tomato leaves. II. The cDNA-deduced structure of pre-inhibitor II. Journal of Biological Chemistry 260, 6561–6564.
Griffiths, D.W. (1984) The trypsin and chymotrypsin inhibitor activities of various pea (Pisum spp.) and field bean (Vicia faba) cultivars. Journal of the Science of Food and Agriculture 35, 481–486.
Hilder, V.A., Gatehouse, A.M.R., Sheerman, S.E., Barker, R.F. and Boulter, D. (1987) A novel mechanism of insect resistance engineered into tobacco. Nature 330, 160–163.
Kakade, M.L., Rackis, J.J., McGhee, J.E. and Puski, G. (1974) Determination of trypsin inhibitor activity of soy products: a collaborative analysis of an improved procedure. Cereal Chemistry 51, 376–382.
Leterme, P., Beckers, Y. and Théwis, A. (1989) Inter- and intravarietal variability of the trypsin inhibitor content of peas and its influence on apparent digestibility of crude proteins by growing pigs. pp. 121–124 in Huisman, J., van der Poel, T.F.B. and Liener, I.E. (Eds) Recent advances of research in antinutritional factors in legume seeds. Wageningen PUDOC.
Liener, I.E. and Hasdai, A. (1986) The effect of the long-term feeding of raw soy flour on the pancreas of the mouse and hamster. Advances in Experimental Medicine and Biology 199, 189–198.
Liener, I.E. and Kakade, M.L. (1980) Protease inhibitors. pp. 7–71 in Liener, I.E. (Ed.) Toxic constituents of plant foodstuffs. New York, Academic Press.
Matthews, P. and Arthur, A.E. (1985) Genetic and environmental components of variation in protein content of peas. pp. 369–381 in Hebblethwaite, P.D., Heath, M.C. and Dawkins, T.C.K. (Eds) The pea crop. London Butterworths.
Pate, J.S. (1985) Physiology of pea — a comparison with other legumes in terms of economy of carbon and nitrogen in whole-plant and organ functioning. pp. 279–296 in Hebblethwaite, P.D., Heath, M.C. and Dawkins, T.C.K. (Eds) The pea crop. London Butterworths.
Poerio, E., Carrano, L., Garzillo, A.M. and Buonocore, V. (1989) A trypsin inhibitor from the water-soluble protein fraction of wheat kernel. Phytochemistry 28, 1307–1311.
Preston, K. and Kruger, J. (1976) Location and activity of proteolytic enzymes in developing wheat kernels. Canadian Journal of Plant Science 56, 217–223.
Richardson, M. (1991) Seed storage proteins: the enzyme inhibitors. Methods in Plant Biochemistry 5, 259–305.
Savage, G.P. (1989) Antinutritive factors in peas. pp. 342–350 in Huisman, J., van der Poel, T.F.B. and Liener, I.E. (Eds) Recent advances of research in antinutritional factors in legume seeds. Wageningen PUDOC.
Stauffer, C.E. (1990) Measuring trypsin inhibitor in soy meal: suggested improvements in the standard method. Cereal Chemistry 67, 296–302.
Valdebouze, P., Bergeron, E., Gaborit, T. and Delort-Laval, J. (1980) Content and distribution of trypsin inhibitors and hemagglutinins in some legume seeds. Canadian Journal of Plant Science 60, 695–701.
Van Oort, M.G., Hamer, R.J. and Slager, E.A. (1989) The trypsin inhibitor assay: improvement of an existing method. pp. 110–113 in Huisman, J., van der Poel, T.F.B. and Liener, I.E. (Eds) Recent advances of research in antinutritional factors in legume seeds. Wageningen, PUDOC.
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Seed Science Research
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