Abstract
The lipotropic hormone β-lipotropin (β-LPH) was first isolated in 1964 from sheep pituitaries (Li, 1964). It is located in discrete cells of the anterior and intermediate lobes of the pituitary (Moon et al., 1973). β-LPH consists of 90 or 91 amino acids and the sequence does not vary much among the species (Li and Chung, 1976). The residues 41–58 resemble those found in the melanocyte stimulating hormone β-MSH (table 16.1). Thus, β-LPH may be a pro-hormone for this polypeptide. Other β-LPH fragments were recently found in pituitary material and each of the various peptides generated from β-LPH seems to be formed by cleavage of the lipotropin chain at the carboxyl side of paired basic residues (Bradbury et al., 1976a). Residues 47–53 are identical to residues 4–10 that are found in adrenocorticotropic hormone (ACTH) and in α- and β-MSH. This sequence has not been found in pituitary extracts but this or a related peptide could well be generated from β-LPH, ACTH, α- or β-MSH.
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de Wied, D. (1978). Behavioural effects of neuropeptides related to ß-LPH. In: Hughes, J. (eds) Centrally Acting Peptides. Biological Council. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-03668-4_16
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