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The Segment Assay of the Adrenocorticotrophic Hormone

  • Joseph Chayen
Part of the Monographs on Endocrinology book series (ENDOCRINOLOGY, volume 17)

Abstract

Until recently ACTH was regarded as a single, well-defined polypeptide of 39 amino acids. The structure of ACTH derived from the pituitary gland of several species, its physical chemistry and possible three-dimensional structure and conformational changes, have been reviewed by Schwyzer (1977; also see Ney et al. 1964). However, as shown by Orth and Nicholson (1977) it now seems to be only a ‘central element in a wide array of biosynthetically-related polypeptides’. The potential precursor of all these hormones may be big ACTH (Rees 1977) or very big ACTH (Orth and Nicholson 1977) so that the lipotrophins (the large β h -LPH and the γ h -LPH), ACTH, the endorphins, α- and β-MSH, and the ACTH-like intermediate lobe peptide (CLIP) are all related. Thus α-enkephalin corresponds to β-LPH61–65; β-endorphin to β-LPH61–91; β-MSH which, in the human but not in other species, now seems to be an extraction artefact (Rees, 1977) corresponds to β-LPH41–58 while α-MSH is equivalent to N-α-acetyl [ACTH1–13]-NH2; and CLIP is ACTH18–39 (Orth and Nicholson 1977; Rees 1977). The possible relationships have been discussed by Smyth (1978) and are shown in Fig. 7.1.

Keywords

Adrenal Gland Adrenocorticotrophic Hormone Adrenal Cortex Prussian Blue Zona Fasciculata 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer-Verlag Berlin, Heidelberg 1980

Authors and Affiliations

  • Joseph Chayen
    • 1
  1. 1.Division of Cellular BiologyThe Mathilda and Terence Kennedy Institute of RheumatologyLondonUK

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