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The amino acid sequence of peanut agglutinin.
- Source :
-
European Journal of Biochemistry . 3/28/91, Vol. 196 Issue 3, p631-637. 7p. - Publication Year :
- 1991
-
Abstract
- The amino acid sequence of peanut (Arachis hypogaea) agglutinin was determined from three major fragments obtained by mild acid cleavage at Asp-Pro peptide bonds. The sequence of 236 amino acids has residues identical to those that form the metal-binding site and the hydrophobic pocket in concanavalin A and other lectins, although the overall similarity is only 42%. In the segments of peanut agglutinin that correspond to the four loops that form the carbohydrate-binding site in concanavalin A and ravin, several central residues are homologous, while others show changes to smaller side chains, such as Tyr → Gly. The carbohydrate-binding site of peanut agglutinin may therefore have a similar peptide-backbone architecture, but form a considerably more open cleft. [ABSTRACT FROM AUTHOR]
- Subjects :
- *PEANUTS
*AGGLUTININS
*AMINO acid sequence
*PEPTIDES
*BINDING sites
*LECTINS
Subjects
Details
- Language :
- English
- ISSN :
- 00142956
- Volume :
- 196
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- European Journal of Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 13674900
- Full Text :
- https://doi.org/10.1111/j.1432-1033.1991.tb15859.x