Molecular forms of β-endorphin in the canine pituitary gland
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Summary
Acid extracts of anterior and intermediate lobes of the pituitary gland from 4 dogs were fractionated by cation-exchange high-performance liquid chromatography and analzyed by radioimmunoassay, using 2 antibodies: one specific for the midregion of β-endorphin (β-end) and the other specific for the N-terminal region of N-acetylated β-end. Identification of peaks of canine β-end immunoreactivity was based on the retention times relative to those of synthetic human β-end standards, with predicted variations attributable to differences in the β-end amino acid sequences between the 2 species. The canine anterior lobe was found to contain almost exclusively β-end (1–31). By contrast, the intermediate lobe contained substantial amounts of N-acetylated and C-terminally shortened forms of β-end. The predominant forms of β-end in canine intermediate lobe were, in decreasing order of abundance: β-end (1–27), β-end (1–31), β-end (1-26), Acβ-end (1–27), Acβ-end (1–26) and Acβ-end (1–31). Individual β-end immunoreactivity profiles varied, but the general pattern was consistent among the 4 dogs.
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