期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1970
卷号：65
期号：3
页码：745-752
DOI：10.1073/pnas.65.3.745
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Pure monoiodo ACTH-125I was prepared that was biologically active and free of unlabeled ACTH. Extracts of adrenal cortex that contained ACTH-sensitive adenyl cyclase, bound ACTH-125I; extracts that lacked the ACTH-sensitive cyclase did not bind ACTH-125I. Unlabeled ACTH inhibited the binding of ACTH-125I. Five ACTH derivatives which varied widely in biological activity were tested. All inhibited the binding of ACTH-125I 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-125I. This study demonstrates directly the binding of ACTH to its biologically significant site.
