Abstract
Calf anterior pituitaries were defatted and homogenized and peptides were adsorbed from the homogenate supernatant onto octadecylsilyl-silica. After elution, the resulting extract was subjected to gradient elution reversed-phase high pressure liquid chromatography (RP-HPLC) using aqueous acetonitrile containing 0.1% ( v v ) trifluoroacetic acid (TFA). Radioimmunoassay of column fractions for corticotropin (ACTH) revealed three major areas of immunoreactivity. Each was purified to homogeneity by gradient elution RP-HPLC employing aqueous acetonitrile containing either 0.13% heptafluorobutyric acid ( v v ) or 0.1% TFA ( v v ). Amino acid analysis and exopeptidase and trypsin digestions revealed the three forms of corticotropin to be ACTH 1–38, corticotropin-like intermediary lobe peptide, (CLIP, ACTH 18–39) and ACTH 1–39. 3H-labeled ACTH 1–39 did not give rise to either 3H-ACTH 1–38 or 3H-CLIP during isolation.
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