To begin to define the nature of the biosynthesis and processing of ACTH and beta-endorphin in the human, anterior pituitary tissue (fresh normal and adenomatous, and autopsy) was extracted in acetic acid in the presence of protease inhibitors and subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The gel slice eluates were assayed for ACTH and beta-endorphin immunoactivity. Human anterior pituitary tissue contained four major size classes of ACTH and three major size classes of beta-endorphin. We found that in all tissue sources examined there was a virtual absence of 13-15K ACTH, which is a major form in the rat and mouse. When comparing extracts obtained from fresh normal or adenomatous anterior pituitary tissue, we also found a drastic decrease in beta-lipotropin and beta-endorphin in extracts of autopsy human anterior pituitaries. These results suggest that the biosynthesis and processing of pituitary ACTH and beta-endorphin in the human may be different than in the mouse, and because of apparent postmortem proteolysis of beta-endorphin, human pituitary obtained at autopsy is probably not a good source of material for biochemical studies of pituitary tissue.
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