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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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1
Department of Biophysics, Weizmann Institute of Science, Rehovot, Israel.

Erratum in

  • FEBS Lett 1990 Feb 12;261(1):217.

Abstract

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.

PMID:
2806566
DOI:
10.1016/0014-5793(89)81791-0
[Indexed for MEDLINE]
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