This paper describes a simple means of obtaining high resolution separations of basic proteins at a pH below their pl. Small amounts of a cationic fluorosurfactant are added to the running buffer. A positively charged wall is thereby obtained which will repel positively charged proteins. The particular chemistry of fluorosurfactants is believed to enhance the efficiency of the deactivation. Examples are presented of the separation of some model proteins, including a human insulin‐like growth factor (IGF‐I), and a misfolded by‐product of the growth factor.
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Emmer et al. (1991) studied this question.
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