• Media type: E-Article
  • Title: Carbohydrate binding properties of banana (Musa acuminata) lectin : II. Binding of laminaribiose oligosaccharides and β‐glucans containing β1,6‐glucosyl end groups : <b>II. Binding of laminaribiose oligosaccharides and β‐glucans containing β1,6‐glucosyl end groups</b>
  • Contributor: Goldstein, Irwin J.; Winter, Harry C.; Mo, Hanqing; Misaki, Akira; Van Damme, Els J. M.; Peumans, Willy J.
  • imprint: Wiley, 2001
  • Published in: European Journal of Biochemistry
  • Language: English
  • DOI: 10.1046/j.1432-1327.2001.02149.x
  • ISSN: 0014-2956; 1432-1033
  • Keywords: Biochemistry
  • Origination:
  • Footnote:
  • Description: <jats:p>This paper extends our knowledge of the rather bizarre carbohydrate binding poperties of the banana lectin (<jats:italic>Musa acuminata</jats:italic>). Although a glucose/mannose binding protein which recognizes α‐linked <jats:italic>gluco</jats:italic>‐and <jats:italic>manno</jats:italic>‐pyranosyl groups of polysaccharide chain ends, the banana lectin was shown to bind to internal 3‐<jats:italic>O</jats:italic>‐α‐<jats:sc>d</jats:sc>‐glucopyranosyl units. Now we report that this lectin also binds to the reducing glucosyl groups of β‐1,3‐linked glucosyl oligosaccharides (e.g. laminaribiose oligomers). Additionally, banana lectin also recognizes β1,6‐linked glucosyl end groups (gentiobiosyl groups) as occur in many fungal β1,3/1,6‐linked polysaccharides. This behavior clearly distinguishes the banana lectin from other mannose/glucose binding lectins, such as concanavalin A and the pea, lentil and <jats:italic>Calystegia sepium</jats:italic> lectins.</jats:p>
  • Access State: Open Access