The amino acid sequences of the alpha 1 and alpha 2 subunits of the isolectins from seeds of Lathyrus ochrus (L) DC.
The complete amino acid sequences of the alpha 1 and alpha 2 subunits of the isolectins (LoL I and LoL II) from seeds of Lathyrus ochrus were determined by analysis of peptides derived from the proteins by digestion with trypsin, chymotrypsin and the S. aureus V8 protease. Both subunits consisted of single polypeptide chains of 53 amino acids, which differed from one another in only 4 positions near their C-termini, and exhibited high homology to the light (alpha) chains of the lectins from Lathyrus sativus, L. odoratus and a number of other legume seeds.
D000595:Amino Acid Sequence; D002918:Chymotrypsin; D010450:Endopeptidases; D037102:Lectins / Q000302:isolation & purification*; D046911:Macromolecular Substances; D010446:Peptide Fragments / Q000032:analysis; D037121:Plant Lectins; D012697:Serine Endopeptidases; D014357:Trypsin
D037102:Lectins; D046911:Macromolecular Substances; D010446:Peptide Fragments; D037121:Plant Lectins; C039412:lathyrus lectin; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C028344:glutamyl endopeptidase; D014357:Trypsin