ISOLATION, AMINO ACID SEQUENCE AND ACTION OF GUINEA-PIG ACTH ON ALDOSTERONE PRODUCTION BY GLOMERULOSA CELLS

Abstract

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 [ill] 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.