Abstract
1. 1. Hemoglobins from more than fifty species and subspecies of turtles were examined by starch-gel electophoresis at pH 7·0, 8·4 and 9·5. The hemoglobins were reduced with mercaptoethanol, and then reacted with iodoacetamide in order to dissociate any polymeric molecules and to prevent their formation. The polypeptide chains were examined at pH 1·8 after reduction and reaction with iodoacetamide in 8 M urea at pH 7·0. 2. 2. Most species examined have two major and one or more minor hemoglobin components. Three distinct polypeptide chains can be resolved at pH 1·8.
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