Isolation, amino acid sequence and action of guinea-pig ACTH on aldosterone production by glomerulosa cells.
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.
Smith
A I
AI
Medical Research Centre, Prince Henry's Hospital, Melbourne, Australia.
Wallace
C A
CA
Moritz
R L
RL
Simpson
R J
RJ
Schmauk-White
L B
LB
Woodcock
E A
EA
Funder
J W
JW
D000302:Adrenal Cortex / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D000324:Adrenocorticotropic Hormone / Q000302:isolation & purification* / Q000494:pharmacology; D000450:Aldosterone / Q000096:biosynthesis*; D000595:Amino Acid Sequence; D000818:Animals; D006168:Guinea Pigs; D008969:Molecular Sequence Data
D000450:Aldosterone; D000324:Adrenocorticotropic Hormone