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Clinical Chemistry 43: 950-956, 1997;
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(Clinical Chemistry. 1997;43:950-956.)
© 1997 American Association for Clinical Chemistry, Inc.

Articles

Growth hormone (GH) assays: influence of standard preparations, GH isoforms, assay characteristics, and GH-binding protein

Chatarina Jansson1,a, Cesar Boguszewski2, Sten Rosberg1, Lena Carlsson2 and Kerstin Albertsson-Wikland1

1 International Pediatric Growth Research Centre, Department of Pediatrics, and
2 Research Centre for Endocrinology and Metabolism, Department of Internal Medicine, University of Göteborg, Göteborg, Sweden.
a Address correspondence to this author at: Int. Pediatric Growth Research Centre, Department of Pediatrics, Children's Hospital, S-416 85 Göteborg, Sweden. Fax +46 31 848952; e-mail chatarina.jansson{at}pediat.gu.se

The impact of the adoption of the new biosynthetic growth hormone (GH) WHO International Reference Preparation (IRP 88/624), and the recommendation to report results in µg/L instead of mU/L, is described. Conversion factors were determined by comparing both the linear and nonlinear relations of the GH values. The Pharmacia polyclonal IRMA (p-IRMA) and the DELFIA® monoclonal time-resolved immunofluorometric assay (trIFMA) with kit calibrators calibrated either against the pituitary-derived WHO IRP 80/505 or the new 88/624 were evaluated. Conversion factors of 4.17 mU/L = 1 µg/L for the p-IRMA and 4.31 mU/L = 1 µg/L for the trIFMA were necessary. Different cross-reactivity patterns for the deaminated and dimer 22-kDa, 20-kDa, and 17-kDa GH isoforms were found. Expected GH recovery was similar when the measured values were adjusted according to the results of the cross-reactivity study.


Key Words: indexing terms: conversion factors • immunoassays • antibodies




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Copyright © 1997 by the American Association for Clinical Chemistry.