Isolation and characterization of BanLec-I, a mannoside-binding lectin from Musa paradisiac (banana).
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.
Koshte
V L
VL
Central Laboratory of The Netherlands Red Cross Blood Transfusion Service, Amsterdam.
van Dijk
W
W
van der Stelt
M E
ME
Aalberse
R C
RC
D000818:Animals; D002850:Chromatography, Gel; D005638:Fruit; D006384:Hemagglutination; D006801:Humans; D037102:Lectins / Q000302:isolation & purification*; D008213:Lymphocyte Activation; D008358:Mannose; D008970:Molecular Weight; D037121:Plant Lectins; D011863:Radioimmunoassay; D013601:T-Lymphocytes / Q000276:immunology
C066788:BanLec-I; D037102:Lectins; D037121:Plant Lectins; D008358:Mannose