Isolation and characterization of BanLec-I, a mannoside-binding lectin from Musa paradisiac (banana)

Biochem J. 1990 Dec 15;272(3):721-6. doi: 10.1042/bj2720721.


A lectin (BanLec-I) from banana (Musa paradisiac) with a binding specificity for oligomannosidic glycans of size classes higher than (Man)6GlcNAc was isolated and purified by affinity chromatography on a Sephadex G-75 column. It did not agglutinate untreated human or sheep erythrocytes, but it did agglutinate rabbit erythrocytes. BanLec-I stimulated T-cell proliferation. On size-exclusion chromatography, BanLec-I has a molecular mass of approx. 27 kDa, and on SDS/PAGE the molecular mass is approx. 13 kDa. The isoelectric point is 7.2-7.5. BanLec-I was found to be very effective as a probe in detecting glycoproteins, e.g. on nitrocellulose blots.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Chromatography, Gel
  • Fruit*
  • Hemagglutination
  • Humans
  • Lectins / isolation & purification*
  • Lymphocyte Activation
  • Mannose*
  • Molecular Weight
  • Plant Lectins
  • Radioimmunoassay
  • T-Lymphocytes / immunology


  • BanLec-I
  • Lectins
  • Plant Lectins
  • Mannose