Single step purification, characterization and N-terminal sequences of a mannose specific lectin from mulberry seeds

A mannose/glucose specific lectin have been isolated and purified from mulberry seeds by affinity chromatography on ConA Sepharose. The lectin is monomer in nature as judged by SDS-PAGE and its MW was estimated to be 22,000. The lectin is glycoprotein with neutral sugar content of 28.57%, and mannos...

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Bibliographic Details
Published in:The Protein Journal 2005-08, Vol.24 (6), p.369-377
Main Authors: Absar, Nurul, Yeasmin, T, Raza, M Salim, Sarkar, S Kumar, Arisaka, F
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Artemia
Bacteria
Bioassays
Carbohydrates - analysis
Chromatography, Affinity
Hemagglutination
Mannose-Binding Lectins - chemistry
Mannose-Binding Lectins - isolation & purification
Mannose-Binding Lectins - toxicity
Molecular Weight
Morus - chemistry
Plant Lectins - chemistry
Plant Lectins - isolation & purification
Poisoning
Rats
Seeds - chemistry
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Summary:A mannose/glucose specific lectin have been isolated and purified from mulberry seeds by affinity chromatography on ConA Sepharose. The lectin is monomer in nature as judged by SDS-PAGE and its MW was estimated to be 22,000. The lectin is glycoprotein with neutral sugar content of 28.57%, and mannose and glucose were identified as carbohydrate. The lectin agglutinated rat red blood cells and in a hapten inhibition test, D: -mannose and D: -glucose was found to be inhibitor. The lectin also exhibited cytotoxic effect in brine shrimp lethality bioassay. The N-terminal sequences of the lectin upto 45-residues except the positions of 21, 39, 42 and 44 were identified. Sequence homology of the lectin is also discussed.
ISSN:1572-3887
1875-8355
1573-4943
DOI:10.1007/s10930-005-7590-6