Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/32216
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Título : Modification of the amino and hydroxyl groups of lysozyme with carboxylic acid anhydrides: a comparative study
Autor : Bernad, Antonio, Nieto, M. Ángela, Vioque, Agustín, Palacián, Enrique
Palabras clave : Lysozyme
Chemical modification
Carboxylic acid anhydride
Lysine residue
Serine residue
Threonine residue
Hydroxyl group regeneration
Fecha de publicación : 17-Oct-1986
Editor: Elsevier
Citación : Biochimica et Biophysica Acta 873(3): 350-355 (1986)
Resumen: Modification of hydroxyl groups by carboxylic acid anhydrides is an unwanted reaction when these reagents are used to modify protein amino groups. It is important to know the specificity of different anhydrides, and the stability of the modified hydroxyl groups. Lysozyme was treated with acetic, succinic, maleic, monomethylmaleic and dimethylmaleic anhydrides, and the extent of modification of the amino and hydroxyl groups was evaluated. Amino groups were found to be much more reactive than the hydroxyl groups. Of the reagents used, dimethylmaleic anhydride is the most specific for amino groups, with practically no modification of hydroxyamino acid residues. The modified hydroxyl groups are preferentially deacylated at alkaline pH. For acetic, succinic and maleic anhydrides, the half-lives of the modified serine (25–45 min) and threonine (14–30 h) residues were determined at pH 10.0 and 37°C. Under these conditions, the modified hydroxyl groups can be selectively deacylated without practically affecting the modified amino groups.
Descripción : 6 páginas, 4 figuras, 1 tabla.
Versión del editor: http://dx.doi.org/10.1016/0167-4838(86)90083-X
URI : http://hdl.handle.net/10261/32216
ISSN: 0006-3002
DOI: 10.1016/0167-4838(86)90083-X
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