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FEBS Lett. 1989 Oct 23;257(1):81-5.

The amino acid sequence of Erythrina corallodendron lectin and its homology with other legume lectins.

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Department of Biophysics, Weizmann Institute of Science, Rehovot, Israel.

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  • FEBS Lett 1990 Feb 12;261(1):217.


The primary sequence of Erythrina corallodendron lectin was deduced from analysis of the peptides derived from the lectin by digestion with trypsin, chymotrypsin, Staphylococcus aureus V8 protease, elastase and lysylendopeptidase-C, and of fragments generated by cleavage of the lectin with dilute formic acid in 6 M guanidine hydrochloride. Purification of the individual peptides was achieved by gel filtration, followed by reverse phase HPLC. The glycosylation site (Asn17-Leu18-Thr19) was deduced from analysis of the glycopeptide isolated from a pronase digest of the lectin before and after deglycosylation of the glycopeptide with endoglycosidase F. Comparison of the sequence of 244 residues thus obtained with those of 9 other legume lectins revealed extensive homologies, including 39 invariant positions and 60 partial identities. These data provide further evidence for the conservation of the lectin gene in leguminous plants.

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