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Antinutritional and Biochemical Properties of Winged Bean Trypsin Inhibitors

  • Benito O. de Lumen
  • Jones Chan
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 199)

Abstract

The trypsin inhibitors (TI) of winged bean (Psophocarpus tetragonolobus) isolated by affinity chromatography consisted of 8 protein bands by disc polyacrylamide electrophoresis. All the bands exhibited trypsin inhibitor activity (TIA) with two of the major bands also exhibiting chymotrypsin inhibitor activity (CIA). Electrofocusing separated the TI into 5 protein bands. Two bands with dual TIA/CIA activities had acidic pI while 3 bands with TIA only had alkaline pI. The TI belonged to two molecular weight groups of 20,900 and 16,600, as determined by NaDodSO4 polyacrylamide electrophoresis.

Sufficient quantities of TI were isolated by affinity chromatography for rat feeding. Raw winged bean was toxic to rats, causing death after 12 days of feeding. Autoclaved winged bean was not toxic but caused growth inhibition. When fed with casein, the isolated inhibitor caused slight growth inhibition, pancreatic and spleen hypertrophy. It was concluded that TI in winged bean was not primarily responsible for the toxicity of raw winged bean.

Keywords

Trypsin Inhibitor Trypsin Activity Trypsin Inhibitor Activity Winged Bean Psophocarpus Tetragonolobus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Abbey, B., Neale, R.J., Norton, G., Br. J. Nutr., 1979a, 41:31.CrossRefGoogle Scholar
  2. Abbey, B., Norton, G., Neale, R.J., Br. J. Nutr., 1979b, 41:39.CrossRefGoogle Scholar
  3. Bowman, D.E., Arch Biochem. Biophys., 1971, 144:541.CrossRefGoogle Scholar
  4. Cerny, K., Kordylas, M., Pospisil, F., Svabensky, O., Zajic, D., Br. J. Nutr., 1971, 26:293.CrossRefGoogle Scholar
  5. Cerny, K., Proc. Int. Symp. Dev. Potentials Winged Bean, 1st., 1978, 281.Google Scholar
  6. Davis, B.J., Ann. N.Y. Acad. Sci., 1964, 121:404.CrossRefGoogle Scholar
  7. de Lumen, B.O., Salamat, L.A., Agric. Food Chem., 1980, 28:533.CrossRefGoogle Scholar
  8. Fraenkel-Conrat, H., Bean, R.C., Ducay, E.D., Olcott, H.S., Arch. Biochem. Biophys., 1952, 37:393.CrossRefGoogle Scholar
  9. Gillespie, J.M., Blagrove, R.J., Aust. J. Plant Physiol., 1978, 5:357.CrossRefGoogle Scholar
  10. Gomori, G., Methods Enzymol., 1955, 1:138.CrossRefGoogle Scholar
  11. Haynes, R., Feeney, R.E., J. Biol. Chem., 1967, 242:5378.Google Scholar
  12. Higuchi, M., Suga, M., Iwai, K., Agr. Biol. Chem., 1983, 47:1879–1886.CrossRefGoogle Scholar
  13. Jaffe, W.G., Vega, C.L, J. Nutr., 1968, 94:203.Google Scholar
  14. Jaffe, W.G., Korte, R., Nutr. Rep. Int., 1976, 14:449.Google Scholar
  15. Jones, G., Moore, S., Stein, W.H., Biochemistry, 1963, 2:66.CrossRefGoogle Scholar
  16. Kakade, M.L., Hoffa, D.E., Liener, I.E., J. Nutr., 1973, 103:1772.Google Scholar
  17. Kimura, T., Satanachote, C., Yoshida, A., J. Nutr. Sci. Vitaminol., 1982, 28:27.CrossRefGoogle Scholar
  18. Kortt, A.A., Biochim. Biophys. Acta, 1979, 577:371.CrossRefGoogle Scholar
  19. Liener, I.E., J. Biol. Chem., 1951, 193:183.Google Scholar
  20. Liener, I.E., J. Agric. Food. Chem., 1974, 22:17.CrossRefGoogle Scholar
  21. Liener, I.E., Kakade, M.L., “Protease Inhibitors in Toxic Constituents in Plant Foodstuffs”, Liener, I.E., Ed., Academic Press: New York, 1969, p. 16.Google Scholar
  22. LKB-ProdukterAB, Application Notes, No. 250, Bromma, Sweden, 1977.Google Scholar
  23. Loeffler, L.J., Pierce, J.V., Biochim. Biophys. Acta, 1973, 317:20.CrossRefGoogle Scholar
  24. March, S.C., Parikh, I. Cuatrecasas, P., Anal. Biochem., 1974, 60:149.CrossRefGoogle Scholar
  25. Moore, S., Stein, W.H., Methods Enzymol., 1963, 6:819.CrossRefGoogle Scholar
  26. National Academy of Science “The Winged Bean: A high-protein crop for the tropics”, National Academy of Sciences: Washington, DC, 1975.Google Scholar
  27. Ornstein, L., Ann. N.Y. Acad. Sci., 1964, 121:321.CrossRefGoogle Scholar
  28. Rackis, J., J. Fed. Proc., Fed. Am. Soc. Exp. Biol., 1965, 24:1488.Google Scholar
  29. Richardson, M., Phytochemistry, 1977, 16:159.CrossRefGoogle Scholar
  30. Richardson, M., Food Chem., 1981, 6:235.CrossRefGoogle Scholar
  31. Rosenberg, M., Roegner, V., Becker, F.F., Am. Rev. Respir. Dis., 1976, 113:779.Google Scholar
  32. Roy, D.N., J. Agric. Food Chem., 1980, 28:48.CrossRefGoogle Scholar
  33. Sohonie, K., Bhandakar, A.P., J. Sci. Ind. Res., 1954, 138:500.Google Scholar
  34. Uriel, J., Berges, J., Nature (London), 1968, 218:578.CrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Benito O. de Lumen
    • 1
  • Jones Chan
    • 1
  1. 1.Department of Nutritional SciencesUniversity of CaliforniaBerkeleyUSA

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