Identification and biological activity of lectins of different subunit composition isolated from Phaseolus vulgaris L var athropurpurea
1995
Martinez-Aragon, A. | Cavalle, C. | Fruhbeck, G. | Tosar, A. | Santidrian, S. | Stewart, J.C. | Rubio, L. | Pusztai, A.
Protein concentrate, albumin (AF) and globulin fractions (GF) (60.2, 42.3 and 69.7% of protein content, N x 5.40, respectively) were obtained from raw seeds of Phaseolus vulgaris var athropurpurea (PHVa) cultivated in northern Spain. SDS-PAGE analysis revealed that the isolectins were present solely in the AF while the GF was entirely lectin-free. Affinity chromatography and SDS-PAGE were used to separate and identify lectins of different subunit composition: E4 + E3L, E2L2, E13 and L4 (in g: 0.12, 0.03, 0.03 and 0.44, respectively, from 2.9 g of PHVa meal). In this cultivar the amount of E4 was negligible. With the methodology followed in this study the L4 isolectin could not be isolated from the AF and it was determined by densitometry. The biology activities of these PHVa phytohaemagglutinins-erythroagglutinating and lymphocyte transformation activities-were assessed in rat and human cells. There was a direct correlation between the erythroagglutinating activity and the E subunit composition of the isolectins using rat red blood cells. The lymphocyte transformation activity of the isolectins with human peripheral blood lymphocytes was correlated with the L-subunit content in the lectins. However, the relationship between lymphocyte transformation activity and lectin profile with rat lymphatic node lymphocytes was not as straightforward as expected.
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