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New azobenzene derivatives for directed modification of proteins

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Abstract

Derivatives of azobenzene which contained a maleimide group in one of the benzene rings (for binding to a protein cysteine residue) and maleimide, hydroxyl, or carboxyl substitutes in another benzene ring were synthesized. The reactivity of these compounds towards a cysteine residue of a protein and their optical properties in a free form and after their attachment to the mutant forms of the SsoII restriction endonuclease were studied.

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Abbreviations

NBS:

N-bromosuccinimide

PEG-Mal:

(methylpolyethylenglycol12)3-polyethylenglycol4-maleimide

R.SsoII:

the SsoII restriction endonuclease

SDS:

sodium dodecylsulfate

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Correspondence to T. S. Oretskaya.

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Original Russian Text © Le Thi Hien, B. Schierling, A.Yu. Ryazanova, T.S. Zatsepin, E.M. Volkov, E.A. Kubareva, T.I. Velichko, A. Pingoud, T.S. Oretskaya, 2009, published in Bioorganicheskaya Khimiya, 2009, Vol. 35, No. 5, pp.610–617.

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Hien, L.T., Schierling, B., Ryazanova, A.Y. et al. New azobenzene derivatives for directed modification of proteins. Russ J Bioorg Chem 35, 549–555 (2009). https://doi.org/10.1134/S1068162009050033

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  • DOI: https://doi.org/10.1134/S1068162009050033

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