| Literature DB >> 2268297 |
V L Koshte1, W van Dijk, M E van der Stelt, R C Aalberse.
Abstract
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.Entities:
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Year: 1990 PMID: 2268297 PMCID: PMC1149768 DOI: 10.1042/bj2720721
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857