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Enzyme‐linked immunosorbent assay detection and bioactivity of Cry1Ab protein fragments
Environmental Toxicology and Chemistry
  • Vurtice C. Albright, III, Iowa State University
  • Richard L Hellmich, U.S. Department of Agriculture
  • Joel R. Coats, Iowa State University
Document Type
Article
Publication Version
Published Version
Publication Date
12-1-2016
DOI
10.1002/etc.3497
Abstract

The continuing use of transgenic crops has led to an increased interest in the fate of insecticidal crystalline (Cry) proteins in the environment. Enzyme‐linked immunosorbent assays (ELISAs) have emerged as the preferred detection method for Cry proteins in environmental matrices. Concerns exist that ELISAs are capable of detecting fragments of Cry proteins, which may lead to an overestimation of the concentration of these proteins in the environment. Five model systems were used to generate fragments of the Cry1Ab protein, which were then analyzed by ELISAs and bioassays. Fragments from 4 of the model systems were not detectable by ELISA and did not retain bioactivity. Fragments from the proteinase K model system were detectable by ELISA and retained bioactivity. In most cases, ELISAs appear to provide an accurate estimation of the amount of Cry proteins in the environment, as detectable fragments retained bioactivity and nondetectable fragments did not retain bioactivity.

Comments

This article is published as Albright, Vurtice C., Richard L. Hellmich, and Joel R. Coats. "Enzyme‐linked immunosorbent assay detection and bioactivity of Cry1Ab protein fragments." Environmental toxicology and chemistry 35, no. 12 (2016): 3101-3112. doi: 10.1002/etc.3497.

Rights
Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted.
Language
en
File Format
application/pdf
Citation Information
Vurtice C. Albright, Richard L Hellmich and Joel R. Coats. "Enzyme‐linked immunosorbent assay detection and bioactivity of Cry1Ab protein fragments" Environmental Toxicology and Chemistry Vol. 35 Iss. 12 (2016) p. 3101 - 3112
Available at: http://works.bepress.com/richard_hellmich/151/