Further characterization of glucose-specific peanut root lectin (PRA II).
Amino acid analysis of PRA II, a glucose-specific lectin isolated from 7 day-old peanut seedling roots shows that this lectin is rich in glycyl (103 per mole) and seryl residues (59 per mole), and poor in essential amino acids, the acidic amino acid content is higher than the basic amino acids and that its amino acid composition differs from its seed counterpart (PNA), although neither of the lectins contains cystein. PRA II has two carbohydrate binding sites per molecule as determined by equilibrium dialysis. Modifications of the specific amino acid residues of the lectin with group specific reagents indicate that hydroxyl group of tyrosine is involved in the binding of carbohydrate to PRA II.
Kalsi
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G
Centre for Biochemical Technology, Delhi University Campus.
Das
H R
HR
Das
R H
RH
Babu
C R
CR
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D010367:Arachis; D005947:Glucose; D006384:Hemagglutination; D037102:Lectins / Q000737:chemistry* / Q000302:isolation & purification; D037121:Plant Lectins; D011487:Protein Conformation; D011817:Rabbits
D000596:Amino Acids; D037102:Lectins; D037121:Plant Lectins; D005947:Glucose