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2000
Volume 9, Issue 1
  • ISSN: 0929-8665
  • E-ISSN: 1875-5305

Abstract

A D-glucose / D-mannose specific lectin from seeds of Canavalia grandiflora (ConGF) was purified by affinity chromatography on Sephadex G-50. By SDS-PAGE ConGF yielded three protein bands with apparent molecular masses of 29-30 kDa (α chain), 16-18 kDa (β fragment) and 12-13 kDa (γ fragment), like other related lectins from the genus Canavalia (Leguminosae). ConGF strongly agglutinates rabbit erythrocytes, has a high content of ASP and SER, and its N-terminal sequence (30 residues) is highly similar to the sequences of other related lectins from subtribe Diocleinae.

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/content/journals/ppl/10.2174/0929866023409002
2002-02-01
2025-09-04
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