USE OF A BIOSENSOR WITH SURFACE-PLASMON RESONANCE DETECTION FOR THE DETERMINATION OF BINDING CONSTANTS - MEASUREMENT OF INTERLEUKIN-6 BINDING TO THE SOLUBLE INTERLEUKIN-6 RECEPTOR
Details
Publication Year 1995-03-07, Volume 34, Issue #9, Page 2901-2907
Journal Title
BIOCHEMISTRY
Publication Type
Journal Article
Abstract
The interaction of recombinant human interleukin-6 (IL-6) with the soluble extracellular form of its receptor (sIL-6R) has been characterized by the application of expressions developed for quantitative affinity chromatography to results obtained with a biosensor based on surface plasmon resonance detection. First, the interaction of sIL-6R with IL-6 covalently attached to the biosensor-chip was characterized from the dependence of the surface plasmon resonance response upon the concentration of receptor injected into the biosensor. A binding constant for the interaction between sIL-6R and IL-6 was then determined from the biosensor response observed for mixtures of IL-6 and receptor-a procedure that is shown to provide unequivocal characterization of the competing reaction, irrespective of the model used to describe the biphasic interaction between partitioning receptor and immobilized IL-6. A binding constant of 5 x 10(7) M(-1) has been obtained for the interaction of sIL-6R with two equivalent and independent sites on an essentially dimeric IL-6 preparation produced using the pUC vector system, and also for the interaction of sIL-6R with a monomeric IL-6 preparation that was univalent in its interaction with receptor.
Publisher
AMER CHEMICAL SOC
Keywords
QUANTITATIVE AFFINITY-CHROMATOGRAPHY; RECOMBINANT MURINE INTERLEUKIN-6; PLASMACYTOMA GROWTH-FACTOR; STIMULATORY FACTOR-II; AMINO-ACID-SEQUENCE; MONOCLONAL-ANTIBODY; EQUILIBRIUM PARTITION; SYSTEM; CELLS; MULTIVALENCY
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Creation Date: 1995-03-07 12:00:00
Last Modified: 0001-01-01 12:00:00
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