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. 2014 Dec 5;19(12):20350–20373. doi: 10.3390/molecules191220350

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© 2014 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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(A) NR-SDS-PAGE. The albumin fraction from L. albus seeds (lane 1) was incubated with erythrocyte membranes (lane 2). A 42 kDa subunit was eluted with 0.4 M galactose (lane 3) leaving behind a final membrane fraction (lane 5). Control erythrocyte membranes were treated with galactose (lane 4); (B) Haemagglutination activity of the galactose eluate (GalE, lane 3) was apparent in the first four wells when compared with the negative control (C-; saline); (C) 2-D electrophoretic analysis (2nd dimension performed under reducing conditions) of the 42 kDa subunit reveals the presence of a 30 kDa larger polypeptide (G1) and five isoforms of a smaller (17–18 kDa) polypeptide (G2 to G6). Molecular masses of standards (lane MM) are indicated in kDa. Arrows point to the protein subunit (SDS-PAGE performed under non-reducing conditions) which bound to the erythrocyte membranes.