Affinity patterns of enzyme tracers for triazine immunoassays

Michael G. Weller; Reinhard Niessner

doi:10.1117/12.276170

30 May 1997 Affinity patterns of enzyme tracers for triazine immunoassays

Michael G. Weller, Reinhard Niessner

Proceedings Volume 3105, Chemical, Biochemical and Environmental Fiber Sensors IX; (1997) https://doi.org/10.1117/12.276170
Event: Environmental Sensing III, 1997, Munich, Germany

Abstract

Cross-reactivities are one of the most important characteristics of immunoassays. Nevertheless most cross- reactivity studies are only performed with small molecules, which are similar to the target analyte. The complex mechanism of the binding event of an antibody makes it likely that the orientation of the hapten plays a critical role. Therefore cross-reactivities of hapten-derivatives with spacers may be quite different compared to the simple compound, especially when the spacer has been coupled to a large molecule, like a marker enzyme (e.g. peroxidase). We examined the relative affinity patterns of 17 enzyme tracers to 16 monoclonal and polyclonal antibodies for the analysis of triazine herbicides (atrazine, terbuthylazine, etc.). This allows interesting discussions about the structure of the antibody binding site and the comparison of antibodies generated with different immunogens. In addition, some general rules for the selection of immunogen structures could be derived from the data. The figures shown in this paper facilitate to find suitable tracer haptens for one of the tested antibodies and support for instance the optimization of immunosensor regeneration, as tracer affinity is closely correlated to the dissociation rate constant of an antibody-tracer complex.

Citation Download Citation

Michael G. Weller and Reinhard Niessner "Affinity patterns of enzyme tracers for triazine immunoassays", Proc. SPIE 3105, Chemical, Biochemical and Environmental Fiber Sensors IX, (30 May 1997); https://doi.org/10.1117/12.276170

ACCESS THE FULL ARTICLE

INSTITUTIONAL
Select your institution to access the SPIE Digital Library.

SELECT YOUR INSTITUTION

PERSONAL
Sign in with your SPIE account to access your personal subscriptions or to use specific features such as save to my library, sign up for alerts, save searches, etc.

PERSONAL SIGN IN

No SPIE Account? Create one

PURCHASE THIS CONTENT

SUBSCRIBE TO DIGITAL LIBRARY

50 downloads per 1-year subscription

Members: $195

Non-members: $335 ADD TO CART

25 downloads per 1 - year subscription

Members: $145

Non-members: $250 ADD TO CART

PURCHASE SINGLE ARTICLE

Includes PDF, HTML & Video, when available