Abstract
Summary
Pepsin-treated ACTH materials at approximately 10 times standard were fractionated in a chromatopile using the system butanol-acetic acid-water. The activity was found to be associated with a slow-moving ninhydrin-positive area from which fractions having potencies of about 50 times standard were recovered. No further chromatographic resolution of these fractions was obtained in the solvent systems ordinarily used for amino acids and peptides. In all cases, the activity was associated with ninhydrin-positive areas of the chromatograms.
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