Summary
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.
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References
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 91–99
Brown JWS, Bliss FA, Hall TC (1981) Linkage relationships between genes controlling seed proteins in French Bean. Theor Appl Genet 60: 251–259
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: 263–271
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: 361–367
Cole EW, Fullington JG, Kasarda DD (1981) Grain protein variability among species of Triticum and Aegilops: quantitative SDS-PAGE studies. Theor Appl Genet 60: 17–30
Cuperlovic M, Movsesijan M, Jovanovic B (1982) Immunological quantitation of lectin from Phaseolus vulgaris. Acta Vet (Belgrade) 32: 47–53
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: 549–557
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: 65–71
Goldstein IJ, Hayes CE (1978) The lectins: carbohydratebinding proteins of plants and animals. Adv Carbohydr Chem Biochem 35: 127–340
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, Madison
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: 439–447
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: 353–359
Kroll J (1973) Tandem-crossed immunoelectrophoresis. In: Axelsen NH, Kroll J, Weeke B (eds) A manual of quantitative immunoelectrophoresis. Universitetsforlaget, Oslo, pp 57–59
Laurell CB (1966) Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal Biochem 15: 45–52
Liener IE (1974) Phytohemagglutinins: their nutritional significance. J Agric Food Chem 22: 17–22
Liener IE (1976) Phytohemagglutinins (Phytolectins). Annu Rev Plant Physiol 27: 291–319
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 371–447
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin reagent. J Biol Chem 193: 265–275
Ma Y, Bliss FA (1978) Seed proteins of common bean. Crop Sci 17: 431–437
Mather K (1941) Variation and selection of polygenic characters. J Genet 41: 159–193
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: 1388–1391
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: 1425–1427
Moreira R, Perrone JC (1977) Purification and partial characterization of a lectin from Phaseolus vulgaris. Plant Physiol 59: 783–787
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, Madison
Mutschler MA, Bliss FA (1981) Inheritance of bean seed globulin content and its relationship to protein content and quality. Crop Sci 21: 289–294
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: 547–552
Pusztai A (1980) Nutritional toxicity of the kidney bean (Phaseolus vulgaris). Annu Rep Stud Anim Nutr All Sci 36: 110–118
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: 843–848
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: 677–692
Sullivan JG, Bliss FA (1983) Genetic control of quantitative variation in phaseolin seed protein of common bean. J Am Soc Hortic Sci 108: 782–787
Sun SM, Mutschler MA, Bliss FA, Hall TC (1978) Protein synthesis and accumulation in bean cotyledons during growth. Plant Physiol 61: 918–923
Weeke B (1973) Rocket immunoelectrophoresis. In: Axelsen NH, Kroll J, Weeke B (eds) A manual of quantitative immunoelectrophoresis. Universitetsforlaget, Oslo, pp 37–46
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Communicated by H. F. Linskens
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Osborn, T.C., Brown, J.W.S. & Bliss, F.A. Bean lectins. Theoret. Appl. Genetics 70, 22–31 (1985). https://doi.org/10.1007/BF00264478
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DOI: https://doi.org/10.1007/BF00264478