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Novel peptide surface for reversible immobilization of concanavalin A
Masárová, J., Pure and Applied Biochemistry, LTH, Lund University, S-22100, Sweden, Institute of Chemistry, Slovak Academy of Sciences, SK-84238 Bratislava, Slovakia, Pure and Applied Biochemistry, LTH, Lund Univ., P.O. Box 124, S-22100, Lund, Sweden.
Pure and Applied Biochemistry, LTH, Lund University, S-22100, Sweden.
Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Applied Physics .
Pure and Applied Biochemistry, LTH, Lund University, S-22100, Sweden.
2004 (English)In: Journal of Biochemical and Biophysical Methods, ISSN 0165-022X, E-ISSN 1872-857X, Vol. 60, no 2, p. 163-170Article in journal (Refereed) Published
Abstract [en]

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, p. 163-170
Keywords [en]
Concanavalin A, Hydrophobic interaction, Immobilization, Polymyxin B, Surface plasmon resonance
National Category
Engineering and Technology
Identifiers
URN: urn:nbn:se:liu:diva-45657DOI: 10.1016/j.jbbm.2004.05.005OAI: oai:DiVA.org:liu-45657DiVA, id: diva2:266553
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2017-12-13

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Carlsson, Jenny

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CiteExportLink to record
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  • fi-FI
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  • nn-NB
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  • Other locale
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Output format
  • html
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  • asciidoc
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