The complete amino acid sequence of the major alpha subunit of the lectin from the seeds of Dioclea grandiflora (Mart).
The complete amino acid sequence of the major alpha subunit of the lectin from seeds of Dioclea grandiflora was determined. The sequence was deduced from analysis of peptides derived from the native alpha subunit by digestion with trypsin, chymotrypsin, the Staphylococcus aureus V8 protease, and pepsin; and from larger peptides produced by digestion of the citraconylated protein with trypsin. The alpha subunit consists of a single polypeptide chain of 237 amino acids which differs from the sequence of concanavalin in 53 positions. Significant levels of heterogeneity were observed in five positions in the sequence.
D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D002918:Chymotrypsin; D010450:Endopeptidases; D007887:Fabaceae / Q000032:analysis*; D037102:Lectins / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000032:analysis; D037121:Plant Lectins; D010946:Plants, Medicinal; D012697:Serine Endopeptidases; D014357:Trypsin
C043014:Dioclea grandiflora lectin; D037102:Lectins; D010446:Peptide Fragments; D037121:Plant Lectins; D010450:Endopeptidases; D012697:Serine Endopeptidases; D002918:Chymotrypsin; C028344:glutamyl endopeptidase; D014357:Trypsin