Isolation, amino acid sequence and action of guinea-pig ACTH on aldosterone production by glomerulosa cells

A. I. Smith, C. A. Wallace, R. L. Moritz, R. J. Simpson, L. B. Schmauk-White, E. A. Woodcock, J. W. Funder

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Abstract

Though minor sequence differences between-species have been reported for adrenocorticotrophin, ACTH(1-39), the steroidogenic moiety ACTH(1-24) has appeared invariant in mammals. We here report the isolation, purification and amino acid sequencing of guinea-pig (GP) ACTH in which Pro24 is replaced by Ala24, and the demonstration that GP-ACTH stimulates aldosterone production to maximal levels well above those seen with human ACTH(1-39) or Synacthen, ACTH(1-24) amide, the synthetic ACTH fragment widely used for diagnostic and therapeutic purposes.

Original languageEnglish
JournalJournal of Endocrinology
Volume115
Issue number2
DOIs
Publication statusPublished - 1 Jan 1987

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