Biochemical Journal · 1990 · 78 citations · 14 references
Life SciencesBiochemistryImmunologyGlycobiologyInnate ImmunityProteomicsAffinity ChromatographyCell-surface GlycansGlycan AnalysisGlycan RecognitionGlycan StructureGlycan-protein InteractionsCarbohydrate Binding SpecificityCell Proliferation StimulationIsoelectric PointLectin Affinity ChromatographyLectin Binding SpecificityLectinsMannose-binding LectinsOligomannose Glycans
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.
14
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
Ulrich K. Laemmli · Nature · 1970 · 251.6K citations
Haider Raza, Annie John, Abderrahim Nemmar · Cellular Physiology and Biochemistry · 2013 · 47.3K citations · Full text