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. 1972 Nov;130(2):589–595. doi: 10.1042/bj1300589

Evaluation of 1-fluoro-2-nitro-4-trimethylammoniobenzene iodide, a protein-solubilizing reagent

D A Sutton 1, S E Drewes 1, Ursula Welz 1
PMCID: PMC1174439  PMID: 4664584

Abstract

The new protein reagent 1-fluoro-2-nitro-4-trimethylammoniobenzene iodide reacts with model amino acids to give derivatives that are very stable to hydrolysis. In a dimethyl sulphoxide–water medium it reacts rapidly (3h) with bovine insulin, and substitution occurs quantitatively at the N-terminal amino groups and at the ∈-amino groups of lysine residues. Two of the four tyrosine residues react, and it is assumed that these are the exposed groups leaving the buried groups unattacked. Unlike 1-fluoro-2,4-dinitrobenzene and related reagents, it imparts hydrophilic properties to the protein derivative, thus facilitating structural and other studies on the derivative. Circular-dichroism spectra of the modified insulin suggest that no conformational changes have occurred during reaction. These spectra also reveal the presence of an extrinsic Cotton effect at 410nm.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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