A Monomeric Mannose-Binding Lectin from Inner Shoots of the Edible Chive (Allium tuberosum)
Autor: | Ying-Wai Lam, T. B. Ng |
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Rok vydání: | 2001 |
Předmět: |
Chive
Molecular Sequence Data Ion chromatography Size-exclusion chromatography Biochemistry Mice food Affinity chromatography Lectins Animals Amino Acid Sequence Mannan-binding lectin Gel electrophoresis Chromatography biology Chemistry Hemagglutination food and beverages Lectin biology.organism_classification Allium tuberosum Collectins HIV Reverse Transcriptase food.food Mice Inbred C57BL biology.protein Reverse Transcriptase Inhibitors Allium Mitogens Plant Lectins Carrier Proteins Mannose Plant Shoots Spleen |
Zdroj: | Journal of Protein Chemistry. 20:361-366 |
ISSN: | 1573-4943 0277-8033 |
DOI: | 10.1023/a:1012224602848 |
Popis: | A mannose-binding lectin was isolated from the inner shoots of the chive Allium tuberosum. The procedure involved aqueous extraction, (NH4)2SO4 precipitation, dialysis to remove (NH4)2SO4, affinity chromatography on mannose-agarose, ion exchange chromatography on SP-Sepharose, gel filtration on Superdex 75, and ion exchange chromatography on Mono S. Lectin activity was adsorbed on mannose-agarose, SP-Sepharose, and Mono S. The lectin demonstrated a molecular weight of 13 kDa in sodium dodecyl sulfate-polyacrylamide gel electrophoresis and gel filtration, indicating that it is a single-chain protein. N-terminal sequence analysis revealed its remarkable homology to Allium cepa lectin and similarity to a lesser extent to lectins from members of the Amaryllidaceae, Orchidaceae, and Liliaceae. The lectin manifested mitogenic activity in murine splenocytes and inhibitory activity against human immunodeficiency virus type 1 reverse transcriptase. |
Databáze: | OpenAIRE |
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