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pubmed:abstractText |
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.
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