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      Adrenocorticotropin Radioimmunoassay: Properties of Antisera against Synthetic ACTH(1-24) and Its Clinical Application

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          Abstract

          Two antisera against synthetic ACTH(1-24) developed in rabbit showed strikingly different affinities toward the ACTH molecule. Both antisera (A-6 and A-7) were highly specific for the COOH-terminal region of ACTH(1-24). Antisera A-6 recognized ACTH(1–39) poorly. Radioimmunoassays (RIAs) using these antisera permitted the rapid (≤ 18 h) quantitation of ACTH(1-24) (A-6) or ACTH(1-39) (A-7) at picogram levels. ACTH levels were determined on silicic acid extracts of rat and human plasma samples by the RIA specific for mid-region of ACTH(1-39) (A-7) and compared with that obtained by an ACTH(34–39) (C-terminal) RIA. In nearly all cases the C-terminal/mid-region ACTH ratios were less than 1.0, indicating that C-terminus of ACTH is more readily degraded by tissue or blood peptidases than are internal sequences. A solid-phase immunoadsorbent RIA specific for the extreme COOH-terminus of ACTH(1-24) was developed by coupling antiserum (A-6) to Sepharose 4B. This assay exhibited the same specificity as the soluble antiserum, yet tolerated relatively high concentrations of protein. Although the assay was suitable for rapid quantitation of ACTH(1-24), a decrease in sensitivity was observed in comparison to a conventional assay.

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          Author and article information

          Journal
          HRE
          10.1159/issn.0018-5051
          Hormone Research in Paediatrics
          S. Karger AG
          0018-5051
          2571-6603
          1984
          1984
          26 November 2008
          : 20
          : 2
          : 129-137
          Affiliations
          aEndocrinology Group, Laboratory of Pulmonary Function and Toxicology, National Institute of Environmental Health Sciences, Research Triangle Park, N.C., USA; bDepartment of Medicine, University of North Carolina, Chapel Hill, N.C., USA
          Article
          179985 Horm Res 1984;20:129–137
          10.1159/000179985
          © 1984 S. Karger AG, Basel

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          Page count
          Pages: 9
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