Abstract
The proteins in wools obtained from copper.deficient sheep before and after supplementing the diet with copper have been solubilized with urea-potassium thioglycollate at pH II, alkylated with iodoacetate, and then separated into protein fractions of high- and low-sulphur content. The isolated proteins from these wools have been examined by moving boundary electrophoresis and the mobilities and relative proportions of the various components measured.

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