Abstract
β-Endorphin, a 31-residue peptide with potent analgesic activity, was first isolated from pituitary glands when it was found to coexist with a related peptide, β-endorphin1-27, which possessed only slight analgesic activity (Bradbury et al., 1975; Smyth et al., 1978). This finding, that a hormone can exist in inactive as well as active forms, did not appear to have a precedent, and it was compounded when the two peptides were seen to occur also in α,N-acetylated forms that were devoid of opiate activity (Smyth et al., 1979). Subsequently, it was found that β-endorphin is derived from a complex prohormone that is the precursor of several biologically active peptides (Roberts and Herbert, 1977), and this suggested that the specific processing events that give rise to the multiple forms of β-endorphin might be related to the polyfunctional nature of the prohormone.
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© 1986 Plenum Press, New York
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Ham, J., Smyth, D.G. (1986). β-Endorphin. In: Moody, T.W. (eds) Neural and Endocrine Peptides and Receptors. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5152-8_6
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DOI: https://doi.org/10.1007/978-1-4684-5152-8_6
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