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Clinical Chemistry 44: 571-577, 1998;
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Right arrow Endocrinology and Metabolism
(Clinical Chemistry. 1998;44:571-577.)
© 1998 American Association for Clinical Chemistry, Inc.

Endocrinology and Metabolism

Adrenomedullin(1–52) measured in human plasma by radioimmunoassay: plasma concentration, adsorption, and storage

Lynley K. Lewisa, Mary W. Smith, Timothy G. Yandle, A. Mark Richards, and M. Gary Nicholls

a Address correspondence to this author at: Department of Medicine, Christchurch Hospital, PO Box 4345, Christchurch, New Zealand. Fax 64 3 3640 818; e-mail llewis{at}chmeds.ac.nz.

We describe a specific and sensitive RIA for human adrenomedullin (AM)(1–52). The detection limit and the concentration required for 50% inhibition of binding were 0.1 and 1.2 fmol/tube, respectively. Cross-reactivities with AM(1–12), AM(13–52), calcitonin gene-related peptide, amylin, and other vasoactive hormones were negligible. AM immunoreactivity in normal subjects ranged from 2.7 to 10.1 pmol/L (n = 44). We investigated factors influencing the recovery and measurement of AM in the assay. Recovery of labeled AM (>80%) was markedly higher than that of unlabeled AM (56%). Immunoreactivity of exogenous AM added to plasma decreased up to 70% over four freeze–thaw cycles, whereas endogenous AM was stable. Alkali-treated casein (1 g/L) reduced adsorption of AM to surfaces and significantly increased assay precision compared with bovine serum albumin (P <0.0001). HPLC separation of extracted plasma verified the presence of AM(1–52). We suggest that considerable care is needed to ensure that accurate and reproducible results are obtained from studies quantifying this peptide.




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Copyright © 1998 by the American Association for Clinical Chemistry.