Purification and properties of the basic lectins from winged bean seed [Psophocarpus tetragonolobus(L.) DC]

Abstract

The seeds of winged bean, Psophocarpus tetragonolobus (L.) DC, contain a group of acidic lectins (PI z 5.5) and a group of basic lectins (PI > 9.5) characterised by different erythrocyte hemagglutinating specificities. Three basic lectins were separated and purified to apparent homogeneity by chromatography on Ultrogel AcA44 and SP-Sephadex C-25. These lectins are glycoproteins with relative molecular mass of 58 000. The total carbohydrate content of the major lectins, B2 and B3, was 5 % and was comprised of mannose, N-acetylglucosamine, fucose and

Effect of Heat Treatments on Certain Antinutrients and in vitro Protein Digestibility of Peanut and Sesame Seeds

“…A 3% suspension (in PBS, v/v) of washed human erythrocytes, types A, B and O were pretreated with neuraminidase (0.2 units of Sigma Co. N-2876 neuraminidase enzyme per 10 mL blood cell suspension for 1 h at 37℃) then with trypsin (1000 units per 10 mL blood cell suspension for 1 h at 37℃) to assay the lectin activity from peanut seeds. Agglutination was determined using the procedure of Kortt (1984). Starting with 50 μL aliquots of the extracts, serial two-fold dilution were made with PBS in styrene u-well microtiter trays.…”

Localized agglutinin staining in muscle capillaries from normal and very old atrophic human muscle using winged bean ( Psophocarpus tetragonolobus ) lectin

“…The total lectin obtained from seeds of the winged bean contains a group of basic lectins, WBA I (P i >9.5) and a group of acidic lectins, WBA II (P i =5.5). The basic lectins agglutinate human type A and B but not human type 0 trypsinized erythrocytes (Kortt 1984). The acidic lectins agglutinate trypsinized and desialized erythrocytes of all three (A, B, and 0) types (Kortt 1985;Patanjali et al 1988).…”

The 1.8 Å crystal structure of winged bean albumin 1, the major albumin from Psophocarpus tetragonolobus (L.) DC 1 1Edited by K. Nagai

“…The 2 S albumins in winged bean seeds constitute $30% of the seed protein, and include several STI-Kunitz type trypsin inhibitors (Kortt, 1979a;Kortt et al, 1991;Caldwell et al, 1990;Yamamoto et al, 1983), a Bowman-Birk type inhibitor (Kortt, 1978a), a chymotrypsin speci®c inhibitor (Kortt, 1979b), two classes of proteinase (Usha & Singh, 1996) and two lectins (acidic and basic; Kortt, 1984Kortt, , 1985. A preliminary crystallographic study of the basic lectin from winged bean has been published (Sankaranarayanan et al, 1993), and the crystal structure of the winged bean chymotrypsin inhibitor (WCI) has recently been determined (Dattagupta et al, 1990;.…”