Theoretical and Applied Genetics

, Volume 70, Issue 1, pp 22–31 | Cite as

Bean lectins

5. Quantitative genetic variation in seed lectins of Phaseolus vulgaris L. and its relationship to qualitative lectin variation
  • T. C. Osborn
  • J. W. S. Brown
  • F. A. Bliss


Seeds of forty bean cultivars having different lectin types based on two-dimensional isoelectric focusing-sodium dodecyl sulfate polyacrylamide gel electrophoresis (IEF-SDS/PAGE) were analyzed for quantities of lectin, phaseolin and total protein. Significant differences were found among groups of cultivars with different lectin types for the quantity of lectin and phaseolin. Cultivars with more complex lectin types based on IEF-SDS/PAGE tended to have higher quantities of lectin and lower quantities of phaseolin than cultivars with simple lectin types. An association between lectin type and the quantity of lectin and phaseolin was found also in the seeds of F2 plants that segregated in a Mendelian fashion for two lectin types. Seeds from plants with the complex lectin type had more lectin and less phaseolin than seeds from plants with the simple lectin type. Therefore, the genes controlling qualitative lectin variation also may influence the quantitative variation of lectin and phaseolin. The results of this study are related to other studies on the quantitative variation for seed proteins and to the possible molecular basis for variation in the quantity of lectins in beans.

Key words

Phaseolus vulgaris Lectin Phaseolin Quantitative variation Immunoelectrophoresis 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Axelsen NH, Bock E, Kroll J (1973) Comparison of antigens. In: Axelsen NH, Kroll J, Weeke B (eds) A manual of quantitative immunoelectrophoresis. Universitetsforlaget, Oslo, pp 91–99Google Scholar
  2. Brown JWS, Bliss FA, Hall TC (1981) Linkage relationships between genes controlling seed proteins in French Bean. Theor Appl Genet 60: 251–259Google Scholar
  3. Brown JWS, Osborn TC, Bliss FA, Hall TC (1982a) Bean lectins. 1. Relationships between agglutinating activity and electrophoretic variation in the lectin-containing G2/albumin seed proteins of French Bean (Phaseolus vulgaris L.). Theor Appl Genet 62: 263–271Google Scholar
  4. Brown JWS, Osborn TC, Bliss FA, Hall TC (1982b) Bean lectins. 2. Relationship between qualitative lectin variation in Phaseolus vulgaris L. and previous observations on purified bean lectins. Theor Appl Genet 62: 361–367Google Scholar
  5. Cole EW, Fullington JG, Kasarda DD (1981) Grain protein variability among species of Triticum and Aegilops: quantitative SDS-PAGE studies. Theor Appl Genet 60: 17–30Google Scholar
  6. Cuperlovic M, Movsesijan M, Jovanovic B (1982) Immunological quantitation of lectin from Phaseolus vulgaris. Acta Vet (Belgrade) 32: 47–53Google Scholar
  7. Felsted RL, Li J, Pokrywka G, Egorin MJ, Spiegel J, Dale RMK (1981) Comparison of Phaseolus vulgaris cultivars on the basis of isolectin differences. Int J Biochem 13: 549–557Google Scholar
  8. Fullington JG, Cole EW, Kasarda DD (1983) Quantitative sodium dodecyl sulfate-polyacrylamide gel electrophoresis of total proteins extracted from different wheat varieties: effect of protein content. Cereal Chem 60: 65–71Google Scholar
  9. Goldstein IJ, Hayes CE (1978) The lectins: carbohydratebinding proteins of plants and animals. Adv Carbohydr Chem Biochem 35: 127–340Google Scholar
  10. Hartana A (1983) Genetic variability is seed protein levels associated with two phaseolin protein types in common bean (Phaseolus vulgaris L.). MS Thesis, University of Wisconsin, MadisonGoogle Scholar
  11. Jaffe WG, Brücher O, Palozzo A (1972) Detection of four types of specific phytohemagglutinins in different lines of beans (Phaseolus vulgaris). Z Immun-Forsch 142: 439–447Google Scholar
  12. Kitamura K, Kaizuma N (1981) Mutant strains with low level of subunits of 7s globulin in soybean (Glycine max Merr.) seed. Jpn J Breed 31: 353–359Google Scholar
  13. Kroll J (1973) Tandem-crossed immunoelectrophoresis. In: Axelsen NH, Kroll J, Weeke B (eds) A manual of quantitative immunoelectrophoresis. Universitetsforlaget, Oslo, pp 57–59Google Scholar
  14. Laurell CB (1966) Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem 15: 45–52Google Scholar
  15. Liener IE (1974) Phytohemagglutinins: their nutritional significance. J Agric Food Chem 22: 17–22Google Scholar
  16. Liener IE (1976) Phytohemagglutinins (Phytolectins). Annu Rev Plant Physiol 27: 291–319Google Scholar
  17. Lis H, Sharon N (1981) Lectins in higher plants. In: Stumpf PK, Conn EE (eds) The biochemistry of plants, vol VI. Academic Press, London New York, pp 371–447Google Scholar
  18. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin reagent. J Biol Chem 193: 265–275PubMedGoogle Scholar
  19. Ma Y, Bliss FA (1978) Seed proteins of common bean. Crop Sci 17: 431–437Google Scholar
  20. Mather K (1941) Variation and selection of polygenic characters. J Genet 41: 159–193Google Scholar
  21. Miller BJ, Hsu R, Heinrikson R, Yachnin S (1975) Extensive homology between the subunits of the phytohemagglutinin mitogenic proteins derived from Phaseolus vulgaris. Proc Natl Acad Sci USA 72: 1388–1391Google Scholar
  22. Misra PS, Jambunathan R, Mertz ET, Glover DV, Barbosa HM, McWhirter KS (1972) Endosperm protein synthesis in maize mutants with increased lysine content. Science 176: 1425–1427Google Scholar
  23. Moreira R, Perrone JC (1977) Purification and partial characterization of a lectin from Phaseolus vulgaris. Plant Physiol 59: 783–787Google Scholar
  24. Mutschler MA (1979) The genetic control of globulin-1 seed protein, and its relationship to total protein content and quality in the dry bean (Phaseolus vulgaris L.) and male sterility in the dry bean (Phaseolus vulgaris L.). PhD Thesis, University of Wisconsin, MadisonGoogle Scholar
  25. Mutschler MA, Bliss FA (1981) Inheritance of bean seed globulin content and its relationship to protein content and quality. Crop Sci 21: 289–294Google Scholar
  26. Osborn TC, Manen JF, Brown JWS, Bliss FA (1984) Genetic variation in the non-denatured structure of lectins from different Phaseolus vulgaris L. cultivars. Theor Appl Genet 67: 547–552Google Scholar
  27. Pusztai A (1980) Nutritional toxicity of the kidney bean (Phaseolus vulgaris). Annu Rep Stud Anim Nutr All Sci 36: 110–118Google Scholar
  28. Pusztai A, Clarke EMW, King TF, Stewart JC (1979) Nutritional evaluation of kidney beans (Phaseolus vulgaris): chemical composition, lectin content and nutritional value of selected cultivars. J Food Agric 30: 843–848Google Scholar
  29. Shewry PR, Hill JM, Pratt HM, Leggatt MM, Miflin BJ (1978) An evaluation of techniques for the extraction of hordein and glutenin from barley seed and a comparison of the protein composition of ‘Bomi’ and ‘Riso 1508’. J Exp Bot 29: 677–692Google Scholar
  30. Sullivan JG, Bliss FA (1983) Genetic control of quantitative variation in phaseolin seed protein of common bean. J Am Soc Hortic Sci 108: 782–787Google Scholar
  31. Sun SM, Mutschler MA, Bliss FA, Hall TC (1978) Protein synthesis and accumulation in bean cotyledons during growth. Plant Physiol 61: 918–923Google Scholar
  32. Weeke B (1973) Rocket immunoelectrophoresis. In: Axelsen NH, Kroll J, Weeke B (eds) A manual of quantitative immunoelectrophoresis. Universitetsforlaget, Oslo, pp 37–46Google Scholar

Copyright information

© Springer-Verlag 1985

Authors and Affiliations

  • T. C. Osborn
    • 1
  • J. W. S. Brown
    • 1
  • F. A. Bliss
    • 1
  1. 1.Department of HorticultureUniversity of WisconsinMadisonUSA

Personalised recommendations