Abstract
The molecular nature of corticotropin (ACTH)-related peptides in rat brain has been studied using high performance liquid chromatography (HPLC) and radioimmunoassay. The major ACTH-immunoreactive species in rat hypothalamic extracts coelutes with corticotropin-like intermediate lobe peptide (CLIP; ACTH 18–39) on two HPLC solvent gradients, and has 3–4 times more C-terminal than N-terminal immunoreactivity. N-terminal ACTH-immunoreactivity is composed of a number of peaks on HPLC with less than 10% eluting at the position of ACTH. Hypothalamic-C-terminal ACTH immunoreactivity is also heteregeneous and resembles in some respect that seen in the rat neurointermediate lobe. Around 90% of the α-MSH immunoreactivity in the hypothalamus elutes as a single peak in the position of des[N-acetyl]α-MSH (ACTH 1–13-NH 2).
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