BioMed Research International

BioMed Research International / 2004 / Article

Research article | Open Access

Volume 2004 |Article ID 374907 | https://doi.org/10.1155/S1110724304308090

Juliana F. Moura, Luiz DeLacerda, Romolo Sandrini, Fernanda M. Borba, Denise N. Castelo, Elis R. Sade, Sandra Sella, João C. Minozzo, Luis G. Callefe, Bonald C. Figueiredo, "ELISA for Determination of Human Growth Hormone: Recognition of Helix 4 Epitopes", BioMed Research International, vol. 2004, Article ID 374907, 7 pages, 2004. https://doi.org/10.1155/S1110724304308090

ELISA for Determination of Human Growth Hormone: Recognition of Helix 4 Epitopes

Received19 Sep 2003
Revised16 Dec 2003
Accepted22 Dec 2003

Abstract

Human growth hormone (hGH) signal transduction initiates with a receptor dimerization in which one molecule binds to the receptor through sites 1 and 2. A sandwich enzyme-linked immunosorbent assay was developed for quantifying hGH molecules that present helix 4 from binding site 1. For this, horse anti-rhGH antibodies were eluted by an immunoaffinity column constituted by sepharose-rhGH. These antibodies were purified through a second column with synthetic peptide correspondent to hGH helix 4, immobilized to sepharose, and used as capture antibodies. Those that did not recognize synthetic peptide were used as a marker antibody. The working range was of 1.95 to 31.25 ng/mL of hGH. The intra-assay coefficient of variation (CV) was between 4.53% and 6.33%, while the interassay CV was between 6.00% and 8.27%. The recovery range was between 96.0% to 103.8%. There was no cross-reactivity with human prolactin. These features show that our assay is an efficient method for the determination of hGH.

Copyright © 2004 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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