Abstract

The amino acid sequences of the α1 and α2 subunits of the isolectins (LhL1 and LhL2) from seeds of Lathyrus hirsutus and the α subunit of the lectin from L. tingitanus were determined by analysis of peptides derived from the proteins by separate digestions with chymotrypsin and the protease from S. aureus V8. The α1 subunit of the L. hirsutus LhL1 isolectin differed from the α2 form in LhL2 only in having an extra lysine inserted near the C-terminus. The L. tingitanus α subunit differed from the L. hirsutus α1 in three positions and from L. hirsutus α2 in four.

Full Text
Published version (Free)

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call