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

1990; Portland Press; Volume: 272; Issue: 3 Linguagem: Inglês

10.1042/bj2720721

1470-8728

V. Koshte, W. van Dijk, M. E. van der Stelt, Rob C. Aalberse,

Carbohydrate Chemistry and Synthesis

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.