ACTH receptors in the adrenal: specific binding of ACTH-125I and its relation to adenyl cyclase.

Journal Article (Journal Article)

Pure monoiodo ACTH-(125)I was prepared that was biologically active and free of unlabeled ACTH. Extracts of adrenal cortex that contained ACTH-sensitive adenyl cyclase, bound ACTH-(125)I; extracts that lacked the ACTH-sensitive cyclase did not bind ACTH-(125)I. Unlabeled ACTH inhibited the binding of ACTH-(125)I. Five ACTH derivatives which varied widely in biological activity were tested. All inhibited the binding of ACTH-(125)I in direct proportion to their biological activity. Albumin, insulin, and four unrelated iodinated hormones were inert. The addition of excess hormone or acetic acid produced rapid dissociation of bound ACTH-(125)I. This study demonstrates directly the binding of ACTH to its biologically significant site.

Full Text

Duke Authors

Cited Authors

  • Lefkowitz, RJ; Roth, J; Pricer, W; Pastan, I

Published Date

  • March 1, 1970

Published In

Volume / Issue

  • 65 / 3

Start / End Page

  • 745 - 752

PubMed ID

  • 4315615

Pubmed Central ID

  • PMC282969

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.65.3.745


  • eng

Conference Location

  • United States