Skip to main content
Log in

Potentially defensive proteins in mature seeds of 59 species of tropical leguminosae

  • Published:
Journal of Chemical Ecology Aims and scope Submit manuscript

Abstract

A survey of 59 species of tropical legume seeds revealed high interspecific variation in proteinaceous capacity to inhibit bovine trypsin (a digestive enzyme) and to agglutinate human (type B, Rh positive) and laboratory rabbit red blood cells. The legume subfamily Mimosoideae was conspicuous for the absence of seeds with very weak trypsin inhibition. Congenerics sometimes differed strongly from each other with respect to both trypsin inhibition and phytohemagglutination. Half the species of seeds displayed no hemagglutinating capacity with one or the other kinds of red blood cells, and in only 27% of the 30 cases where there was some activity did the same species of seed actively agglutinate both species of red blood cells. A species of seed that had hemagglutinating capacity was almost invariably associated with moderate to high levels of trypsin inactivation. While it has been long known that a great diversity of small toxic and potentially defensive molecules occur in legume seeds and that one species of seed often contains several of them, we now feel that it is reasonable to consider legume seeds as also containing a high diversity of potentially toxic protein molecules. A single seed is likely to contain, at the least, three to four classes of defensive compounds, any or all of which, or some in combination, may be the cause of a seed being rejected by a potential seed predator.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Adams, S.E.I. 1974. Toxic effects ofJatropha curcas in mice.Toxicology 2:67–76.

    Google Scholar 

  • Becker, P.F. 1984. Tannin structure and function: Keeping our perspective.Am. Nat. 124:134–136.

    Google Scholar 

  • Chase, T. Jr., andShaw, E. 1967.p-Nitrophenyl-p′-guanidinobenzoate HCl: A new active site titrant for trypsin.Biochem. Biophys. Res. Commun. 29:508–514.

    Google Scholar 

  • Fellows, L.E., Bell, E.A., Lee, T.S., andJanzen, D.H. 1979. Tetrahydrolathyrine: A new amino acid from seeds ofLonchocarpus costaricensis.Phytochemistry 18:1389–1390.

    Google Scholar 

  • Gatehouse, A.M.R., Gatehouse, J.A., Dobie, P., Kilminster, A.M., andBoulter, D. 1979. Biochemical basis of insect resistance inVigna unguiculata.J. Sci. Food Agric. 30:948–958.

    Google Scholar 

  • Hummel, B. 1959. A modified spectrophotometric determination of chymotrypsin, trypsin and thrombin.Can. J. Biochem. 37:1392–1399.

    Google Scholar 

  • Janzen, D.H. 1969. Seed-eaters versus seed size, number, toxicity and dispersal.Evolution 23:1–27.

    Google Scholar 

  • Janzen, D.H. 1977. How southern cowpea weevil larvae (Bruchidae:Callosobruchus maculatus) die on nonhost seeds.Ecology 58:921–927.

    Google Scholar 

  • Janzen, D.H. 1978. The ecology and evolutionary biology of seed chemistry as relates to seed predation, pp. 163–206,in J.B. Harborne (ed.). Biochemical Aspects of Plant and Animal Coevolution. Academic Press, London.

    Google Scholar 

  • Janzen, D.H. 1981. Lectins and plant-herbivore interactions.Recent Adv. Phytochem. 15:241–258.

    Google Scholar 

  • Janzen, D.H., andHiggins, M.L. 1979. How hard areEnterolobium cyclocarpum (Leguminosae) seeds?Brenesia 16:61–67.

    Google Scholar 

  • Janzen, D.H., andLiesner, R. 1980. Annotated checklist of plants of lowland Guanacaste Province, Costa Rica, exclusive of grasses and nonvascular cryptogams.Brenesia 18:15–90.

    Google Scholar 

  • Janzen, D.H., Juster, H.B., andLiener, I.E. 1976. Insecticidal action of the phytohemagglutinin in black beans on a bruchid beetle.Science 192:795–796.

    Google Scholar 

  • Janzen, D.H., Lynn, D.G., Fellows, L.E., andHallwachs, W. 1982. The indole alkaloid, hypaphorine andPterocarpus seed protection.Phytochemistry 21:1035–1037.

    Google Scholar 

  • Janzen, D.H.,Fellows, L.E.,Bell, E.A., andWaterman, P.J. 1986. Why don't Costa RicanLiomys mice (Heteromyidae) eatLonchocarpus seeds (Leguminosae)? In manuscript.

  • Jayne-Williams, D.J., andBurgess, C.D. 1974. Further observations on the toxicity of navy beans (Phaseolus vulgaris) for Japanese quail (Coturnix coturnix japonica).J. Appl. Bacteriol. 37:149–169.

    Google Scholar 

  • Laskowski, M., andKato, I. 1980. Protein inhibitors of proteinases.Annu. Rev. Biochem. 49:593–626.

    Google Scholar 

  • Lee, D.W. 1979. Biological activity of seed proteins in Malesian legumes.Biotropica 11:214–218.

    Google Scholar 

  • Liener, I.E. 1955. The photometric determination of the hemagglutinating activity of soyin and crude soybean extract.Arch. Biochem. Biophys. 54:223–231.

    Google Scholar 

  • Liener, I.E. 1979. Phytohemagglutinins, pp. 576–618,in G.A. Rosenthal and D.H. Janzen (eds.). Herbivores, Their Interaction with Secondary Plant Metabolites. Academic Press, New York.

    Google Scholar 

  • Olsnes, S., andPihl, A. 1973. Isolation and properties of abrin: A toxic protein inhibiting protein synthesis.Eur. J. Biochem. 35:179–185.

    Google Scholar 

  • Pearce, G., McGinnis, J., andRyan, C.A. 1979. Utilization by chicks of half-cystine from native and denatured proteinase inhibitor protein from potatoes (40415).Proc. Soc. Exp. Biol. Med. 160:180–184.

    Google Scholar 

  • Rosenthal, G.A., andJanzen, D.H. 1983. Avoidence of nonprotein amino acid incorporation into protein by the seed predatorCaryedes brasiliensis (Bruchidae).J. Chem. Ecol. 9:1353–1361.

    Google Scholar 

  • Rosenthal, G.A., andJanzen, D.H. 1985. Ammonia utilization by the bruchid beetleCaryedes brasiliensis (Bruchidae).J. Chem. Ecol. 11:539–544.

    Google Scholar 

  • Rosenthal, G.A., Hughes, C.G., andJanzen, D.H. 1982.L-Canavanine, a dietary nitrogen source for the seed predatorCaryedes brasiliensis (Bruchidae).Science 217:353–355.

    Google Scholar 

  • Rudiger, H. 1984. On the physiological role of plant lectins.Bioscience 54:95–99.

    Google Scholar 

  • Ryan, C.A. 1979. Proteinase inhibitors, pp. 599–618,in G.A. Rosenthal and D.H. Janzen (eds.). Herbivores, Their Interaction with Secondary Plant Metabolites. Academic Press, New York.

    Google Scholar 

  • Stirpe, F., Pession-Brizzi, A., Lorenzoni, E., Strocchi, P., Montanaro, L., andSperti, S. 1976. Studies on the proteins from the seeds ofCroton tiglium and ofJatropha curcas. Toxic properties and inhibition of protein synthesis in vitro.Biochem. J. 156:1–6.

    Google Scholar 

  • Tannous, R.I., andUllah, M. 1969. Effects of autoclaving on nutritional factors in legume seeds.Trop. Agricul. (Trinidad) 46:123–129.

    Google Scholar 

  • Turner, R.H., andLiener, I.E. 1975. The use of glutaraldehyde-treated erythrocytes for assaying the hemagglutinating activity of lectins.Anal. Biochem. 68:651–653.

    Google Scholar 

  • Uy, R., andWold, F. 1977. 1,4-Butanediol diglycyl ether-coupling of carbohydrates to sepharose: Affinity adsorbants for lectins and glycosidases.Anal. Biochem. 81:98–107.

    Google Scholar 

  • Warsy, A.S., Norton, G., andStein M. 1974. Protease inhibitors from broad bean: Isolation and purification.Phytochemistry 12:2481–2486.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

This is Scientific Paper No. 7342, Project 1791, College of Agriculture Research Center, Washington State University.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Janzen, D.H., Ryan, C.A., Liener, I.E. et al. Potentially defensive proteins in mature seeds of 59 species of tropical leguminosae. J Chem Ecol 12, 1469–1480 (1986). https://doi.org/10.1007/BF01012365

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01012365

Key Words

Navigation