Abstract
Insulin, zinc–insulin and iso-insulin were precipitated by cetyltrimethylammonium bromide when the detergent/protein molar ratio was less than 10:1, whereas no precipitation was observed at ratios greater than 10:1. It is concluded that the detergent binds as a dimer at each binding site at ratios greater than 10:1. U.v. difference spectra indicated that the tyrosine residues were perturbed by detergent binding.

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