Isolation and characterization of BanLec-I, a mannoside-binding lectin from Musa paradisiac (banana)
| Autor: | V L Koshte, R C Aalberse, M. E. Van Der Stelt, W. W. van Dijk |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
T-Lymphocytes
Radioimmunoassay BanLec Lymphocyte Activation Biochemistry Gel permeation chromatography Affinity chromatography Lectins Animals Humans Molecular Biology Gel electrophoresis biology Molecular mass Chemistry Hemagglutination food and beverages Lectin Cell Biology Molecular biology Molecular Weight Isoelectric point Sephadex Fruit Chromatography Gel biology.protein Plant Lectins Mannose Research Article |
| Zdroj: | Biochemical Journal. 272:721-726 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2720721 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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