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A sialic acid-binding lectin from the legume Maackia fauriei: comparison with lectins from M-amurensis
- Authors
- Kim, Bum Soo; Oh, Kyung Taik; Cho, Due Hyeon; Kim, Yun Jung; Koo, Wan Mo; Kong, Kwang Hoon; Kim, HaHyung
- Issue Date
- Dec-2004
- Publisher
- ELSEVIER SCI IRELAND LTD
- Keywords
- sialic acid; lectin; bark; Maackia fauriei; legume
- Citation
- PLANT SCIENCE, v.167, no.6, pp 1315 - 1321
- Pages
- 7
- Journal Title
- PLANT SCIENCE
- Volume
- 167
- Number
- 6
- Start Page
- 1315
- End Page
- 1321
- ISSN
- 0168-9452
- Abstract
- A lectin that exhibits hemagglutination activity and cytotoxicity against human cancer cell lines has been purified from the legume Maackia fauriei. This lectin, designated M.fauriei agglutinin (MFA), is a tetramer of 115.6 kDa consisting of 30 kDa subunits with a pl of 4.9. The hemagglutination activity of MFA was inhibited by N-acetylneuraminic acid, Neu5Acalpha2-3Galbeta1-4GlcNAc, and sialoglycoproteins. MFA was stable at pH values from 4.0 to 8.5, and at temperatures below 50degreesC, and its activity was affected by demetalization with EDTA. MFA has a high homology with lectins from M. amurensis-which is the only legume source of lectins that bind to specific carbohydrate chains containing sialic acid-in its N-terminal 20 amino acid sequence. (C) 2004 Elsevier Ireland Ltd. All rights reserved.
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