Isolation and characterization of a lectin from peanut roots.
A glucose-specific lectin has been purified to apparent homogeneity from 7-day-old peanut (Arachis hypogaea) roots by affinity chromatography on a Sephadex G-50. The lectin has a 66 kDa native molecular mass and a 33 kDa subunit molecular mass as revealed by native and denaturing sodium dodecyl sulphate-polyacrylamide gel electrophoresis, respectively. The purified lectin, gives a single precipitin line with the antiserum produced against 7-day-old root extract and shows 5 bands in the pH range of 4.4-5.4 in the isoelectric focusing gel. The glucose-specific lectin activity in the peanut roots appears from the fourth day onwards. Lipopolysaccharides isolated from the host specific Rhizobium strain are a 68-fold more potent inhibitor of the lectin as compared to glucose.
Kalsi
G
G
C.S.I.R. Centre for Biochemicals, Delhi University Campus, India.
Das
H R
HR
Babu
C R
CR
Das
R H
RH
D000818:Animals; D010367:Arachis / Q000737:chemistry*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D005947:Glucose / Q000378:metabolism; D006384:Hemagglutination; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007525:Isoelectric Focusing; D037102:Lectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008345:Manganese / Q000494:pharmacology; D008970:Molecular Weight; D009439:Neuraminidase / Q000494:pharmacology; D019887:Peanut Agglutinin; D037121:Plant Lectins; D011817:Rabbits
D037102:Lectins; D019887:Peanut Agglutinin; D037121:Plant Lectins; D008345:Manganese; D009439:Neuraminidase; D005947:Glucose