American Journal of Sensor Technology. 2014, 2(2), 20-24
DOI: 10.12691/ajst-2-2-2
Open AccessArticle
Mst. Jesmin Sultana1, , Fazle Rabbi Shakil Ahmed2 and M. Taufiq Alam3
1Department of Materials Science & Engineering, Rajshahi University, Rajshahi, Bangladesh
2Department of Pharmacy, Royal Medical Technology Institute, Rajshahi, Bangladesh
3Department of Applied Chemistry & Chemical Engineering, Rajshahi University, Rajshahi, Bangladesh
Pub. Date: April 28, 2014
Cite this paper:
Mst. Jesmin Sultana, Fazle Rabbi Shakil Ahmed and M. Taufiq Alam. Screening and Partial Purification of Lectin from Various Bangladeshi Plant Seeds. American Journal of Sensor Technology. 2014; 2(2):20-24. doi: 10.12691/ajst-2-2-2
Abstract
Lectins are group of proteins or glycoprotein of non immunological origins, which can recognize specific carbohydrate structure. In this research work hemaggulutination was used as technique for screening Bangladeshi vegetables for lectin. Five varieties of legume plant seeds Canavalia gladiata(Sword bean),Lens culinaris (Moshordal), Peasum sativam (Motorsuti), Vigna unguiculata subsp. sesquipedalis (Borboti), Cajanus cajan (Arhordal), one Amaranthaceae Amaranthus caudate (katoadata) and one fruit Citrullus lanatus (Watermelon) species from Bangladesh were examined for lectins with chicken and human erythrocytes. Crude extracts from all the species showed agglutinating activity against the erythrocytes used. The lowest protein concentration required to produce erythrocytes agglutination varied remarkable ranging from 0.7 µg/ml to 8080 µg/ml. The strongest activities were shown in the agglutination of human blood erythrocytes by partial purification of lectin from Moshordal and chicken blood erythrocyte from Katoadata and Sword bean. Inhibition assays performed with mono and disaccharides showed that agglutinating of erythrocytes by Sword bean, Moshordal, Motorsuti and Arhordal extracts were completely inhibited where others three were not inhibited by the sugars. Amonium sulphate at 90% saturation followed by dialysis. Sword bean, Arhordal, Watermelon, Borboti, Motorsuti, Moshordal and Katoadata respectively which correspond to the 144.21 mg, 202.5 mg, 135 mg, 179.4 mg, 6 mg, 288 mg, and 72.8 mg are the total protein content.Keywords:
agglutinating activity partial purification lectins protein content inhibition assays
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References:
| [1] | Sharon, N. (1986) The lectins: Properties and functions and applications in biology and medicine. New York Academic, p. 297-357. |
| |
| [2] | Barondes, S. H. (1984). Science. 223; 1259-1264. |
| |
| [3] | Ashwell, G. and Hardford, J. (1982). Annu. Rev. Biochem. 51; 531-554. |
| |
| [4] | Lipsick, J, S., Beyer, E. C., Barondes, S. H. and Kaplan, N. O. (1980). Biochem. Biophys. Res. Commun. 97; 56-61. |
| |
| [5] | Levi, G., Tarrab- Hazdai, R. and Teichberg, V. I. (1983). Eur. Immunol. 13; 500-507. |
| |
| [6] | Teichberg, V, I., Silman, I., Beitsch, D. D. and Resheff, G. (1975). Proc. Natl, Acad. Sci. U. S. A. 72; 1383-1387. |
| |
| [7] | De Waard, A., Hickman, S. and Kornfeld, S. (1976). J. Bio. Chem. 252; 7581-7587. |
| |
| [8] | Goldstain, I. J., Hughes, R. C., Mongsigny, M., Osawa, T. and Sharon, N. (1980). Nature (London). 285; 66. |
| |
| [9] | Gold, E. R. and Balding, P. (1975). Receptor SpecificProteins. Plant and Animal Lectins. |
| |
| [10] | Yeaton, R. W. (1981). Dev. Comp. Immunol. 5; 391-402. |
| |
| [11] | Gilboa-Garder, N., Susswein, A. J., Mizrahi, L. and Avichezer, D. (1985). FEBS lett. 181; 267-70. |
| |
| [12] | Cohen, E. (1984). Prog. Clini. Biol. Res. 157, New York. Liss pp 207. |
| |
| [13] | Cheng, T. C., Marchlonis, J. J. and Vasta, G. R. (1984). Prog. Clini. Biol. Res. 157, New York. Liss pp. 1-15. |
| |
| [14] | Nicolson, G. L. (1976a). Biochem. Biophys. Acta. 457; 57-108. |
| |