Formation of protein charge ladders by acylation of amino groups on proteins

…, RG Chapman, L Isaacs, GM Whitesides

Index: Colton, Ian J.; Anderson, Janelle R.; Gao, Jinming; Chapman, Robert G.; Isaacs, Lyle; Whitesides, George M. Journal of the American Chemical Society, 1997 , vol. 119, # 52 p. 12701 - 12709

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Citation Number: 54

Abstract

The values of charge and electrophoretic mobility of a protein are changed upon acylation of its α-and Lys ε-NH3+ groups. Partial acylation of the amino groups of a protein results in a set of derivatives that is often resolved by capillary electrophoresis into a set of distinct peaks the “rungs” of a protein charge ladder that differ incrementally in the number of residues modified. Proteins that have values of MW< 50 kD usually form resolved charge ladders ...