Abstract
1. 1.|A new method is described for the isolation and purification of concanavalin A based on its specific adsorption on cross-linked dextran gels and subsequent displacement with d-glucose. 2. 2.|The yield of concanavalin A by this method is approx. 2.0–2.4 g/100 g jack bean meal. The chromatographic recovery is of the order of 94%. 3. 3.|Concanavalin A obtained by this procedure is approx. 98% precipitable with dextran NRRL B-1355-S. 4. 4.|(NH 4) 2SO 4 fractionation of a saline extract of jack bean meal showed the maximum localization of concanavalin A activity to be in the fraction precipitated between 0.50 and 0.60 saturation of (NH 4) 2SO 4. 5. 5.|The nature and specificity of binding of concanavalin A to cross-linked dextran gels have been shown to be generally similar to that of concanavalin A-polysaccharide interaction by demonstrating the reversal of the binding and subsequent elution of the protein from Sephadex G-50 with the same low molecular weight carbohydrates which inhibit concanavalin A-polysaccharide interaction.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Protein Structure
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
