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Auswerteverfahren fuer Bindungsprozesse an Oberflaechen

Determining rate and dissociation constants, useful in binding assays, e.g. of nucleic acids, uses specific differential equations.
 
: Kleinjung, F.; Bier, F.F.

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Frontpage ()

DE 2000-10016656 A: 20000328
DE 2000-10016656 A: 20000328
DE 10016656 A1: 20011004
G01N0033
German
Patent, Electronic Publication
Fraunhofer IBMT ()

Abstract
Die Untersuchung von Bindungskonstanten ist in Chemie und Biologie sowie anverwandten Gebieten von grossem Interesse. Einige Bestimmungsmethoden fixieren einen Bindungspartner auf der Oberflaeche und betrachten die Bindung des anderen Partners an die modifizierte Oberflaeche. Die Erfindung ist ein Auswerteverfahren fuer Bindungsprozesse an Oberflaechen, das Wiederbindungseffekte im mathematischen Konzept der Auswertung beruecksichtigt und dadurch zu korrekten Messwerten fuehrt.

 

DE 10016656 A UPAB: 20011220 NOVELTY - Determining rate constants from data on binding processes that occur at a surface, using a specific differential equation, or dissociation constants from similar data, using a specific differential equation, is new. The integrated forms of the equations may also be used. DETAILED DESCRIPTION - Determining rate constants from data on binding processes that occur at a surface, using a specific differential equation (1), or dissociation constants from similar data, using a specific differential equation (3), is new. The integrated forms of (1) and (3) may also be used. The equations are: dy(t)/dt = -kDy(t) + (ckA + beta kDy(t)) (1-y(t)) f(y) (1) dy(t)/dt = -kDy(t) + beta kDy(t) (1-y(t)) f(y) (3). y(t) = relative surface loading, selected such that loading of all immobilized receptors results in y = 1; t = time; beta = reverse binding constant; kA = association rate; kD = dissociation rate; c = concentration of ligand in the solution at the surface; and f(y) = a function describing the dependence of the effective association rate on the relative surface loading. USE - The method is used to analyze binding and dissociation data for systems where an immobilized receptor binds to its ligand, e.g. in biotechnology, biological analysis, biomedicine, clinical chemistry, diagnosis and sensor technology. ADVANTAGE - The method provides a congruent description of experiments in solution and at a surface. It can include a term that describes the change in surface loading and/or the degree of reverse binding, so eliminates systematic errors in nucleic acid analysis.

: http://publica.fraunhofer.de/documents/N-44760.html