Novel peptide surface for reversible immobilization of concanavalin A
2004 (English)In: Journal of Biochemical and Biophysical Methods, ISSN 0165-022X, Vol. 60, no 2, 163-170 p.Article in journal (Refereed) Published
Concanavalin A (Con A) was spontaneously adsorbed on polymyxin B surface. This peptide-lectin interaction was strong, KD=1.9×10 -10, based predominantly on creation of hydrophobic bonds, and was completely reversible. Concanavalin A on polymyxin B (PmB) retained higher binding capacity for yeast mannan, compared with covalently immobilized lectin. Kinetics of mannan-concanavalin A interaction were significantly different in dependence on type of concanavalin A immobilization. © 2004 Elsevier B.V. All rights reserved.
Place, publisher, year, edition, pages
2004. Vol. 60, no 2, 163-170 p.
Concanavalin A, Hydrophobic interaction, Immobilization, Polymyxin B, Surface plasmon resonance
Engineering and Technology
IdentifiersURN: urn:nbn:se:liu:diva-45657DOI: 10.1016/j.jbbm.2004.05.005OAI: oai:DiVA.org:liu-45657DiVA: diva2:266553