Purification and characterization of two major lectins from Vigna mungo (blackgram)

Suseelan, K. N. ; Bhatia, C. R. ; Mitra, R. (1997) Purification and characterization of two major lectins from Vigna mungo (blackgram) Journal of Biosciences, 22 (4). pp. 439-455. ISSN 0250-5991

PDF - Publisher Version

Official URL: http://www.ias.ac.in/jarch/jbiosci/22/439-455.pdf

Related URL: http://dx.doi.org/10.1007/BF02703190


Blackgram (Vigna mungo L. Hepper) seeds contain two galactose-specific lectins, BGL-I and BGL-II. BGL-I was partially purified into two monomeric lectins which were designated as BGL-I-1 (94 kDa) and BGL-I-2 (89 kDa). BGL-II is a monomeric lectin of 83 kDA. The purified lectins were associated with galactosidase activities. BGL-I-1 and BGL-II were copurified with α-galactosidase activity while BGL-I-2 was largely associated with β-galactosidase activity. These lectins agglutinate trypsin treated rabbit erythrocytes, but not the human erythrocytes of A, B or O groups. They were stable between pH 3.5 and 7.5 for their agglutination. The lectins did not show any metalion requirement. They were inactivated at 50°C. The lectin activity was inhibited by D-galactose (0.1 mM). The Scatchard plots of galactose binding to these lectins are nonlinear and biphasic curves indicative of multiple binding sites. The data show that the monomeric lectins have both lectin and galactosidase activities suggestive of a bifunctional protein.

Item Type:Article
Source:Copyright of this article belongs to Indian Academy of Sciences.
Keywords:Vigna mungo; Legiiminosae; Blackgram; Lectin; Galactosidase
ID Code:82580
Deposited On:13 Feb 2012 07:42
Last Modified:18 May 2016 23:43

Repository Staff Only: item control page