Skip to main navigation Skip to search Skip to main content

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

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

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
Pages (from-to)R5-R8
JournalJournal of Endocrinology
Volume115
Issue number2
DOIs
StatePublished - 1987

Fingerprint

Dive into the research topics of 'Isolation, amino acid sequence and action of guinea-pig ACTH on aldosterone production by glomerulosa cells'. Together they form a unique fingerprint.

Cite this