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

2004 ◽  
Vol 2004 (3) ◽  
pp. 143-149 ◽  
Author(s):  
Juliana F. Moura ◽  
Luiz DeLacerda ◽  
Romolo Sandrini ◽  
Fernanda M. Borba ◽  
Denise N. Castelo ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Synthetic Peptide ◽  
Human Growth ◽  
Cross Reactivity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Immunoaffinity Column ◽  
Receptor Dimerization ◽  
Human Prolactin

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 tohGH 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.

Multiplexed determination of human growth hormone and prolactin at a label free electrochemical immunosensor using dual carbon nanotube–screen printed electrodes modified with gold and PEDOT nanoparticles

The Analyst ◽  
2014 ◽  
Vol 139 (18) ◽  
pp. 4556-4563 ◽  
Author(s):  
V. Serafín ◽  
G. Martínez-García ◽  
L. Agüí ◽  
P. Yáñez-Sedeño ◽  
J. M. Pingarrón
Keyword(s):  
Growth Hormone ◽  
Carbon Nanotube ◽  
Simultaneous Determination ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Electrochemical Immunosensor ◽  
Label Free ◽  
Screen Printed Electrodes ◽  
First Time

A label-free dual electrochemical immunosensor for simultaneous determination of human growth and prolactin hormones was prepared for the first time.

Parallel insulin-like actions of human growth hormone and its part sequence hGH 7–13

1983 ◽  
Vol 102 (4) ◽  
pp. 492-498 ◽  
Author(s):  
John McD. Armstrong ◽  
Joseph Bornstein ◽  
Janet O. Bromley ◽  
S. Lance Macaulay ◽  
Frank M. Ng
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Synthetic Peptide ◽  
Glycogen Synthase ◽  
Human Growth ◽  
Phosphorylase Activity ◽  
Insulin Dependent ◽  
Old Rats ◽  
Insulin Like Activity

Abstract. The insulin-like effects of human growth hormone and the synthetic part sequence, Nα-acetyl-hGH 7–13, on glycogen synthase and phosphorylase have been compared in an in vivo system using 16–18-day-old rats. Both the hormone and its part sequences had similar effects, increasing muscle glycogen synthase a activity and decreasing liver phosphorylase a activity, without affecting phosphorylase activity in muscle or synthase activity in liver. Insulin had similar effects, but also increased liver synthase a activity. The effects of all three substances could be abolished by prior treatment of the animals with anti-insulin serum, showing that the effects of growth hormone and its part sequences were insulin-dependent. Both growth hormone and the synthetic peptide increased the binding of insulin to liver plasma membrane. It is concluded that the insulin-like activity of human growth hormone is associated with a region containing residues 7 to 13 of the hormone molecule, and that this activity is insulin-dependent. It is suggested that both growth hormone and the synthetic peptide produce insulin-like activity by enhancing the binding of circulating insulin to its receptor.

scholarly journals In Silico Investigation of pH-Dependence of Prolactin and Human Growth Hormone Binding to Human Prolactin Receptor

2013 ◽  
Vol 13 (1) ◽  
pp. 207-222 ◽  
Author(s):  
Lin Wang ◽  
Shawn Witham ◽  
Zhe Zhang ◽  
Lin Li ◽  
Michael Hodsdon ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
In Silico ◽  
Ph Dependence ◽  
Prolactin Receptor ◽  
Human Growth ◽  
Chemical Mechanism ◽  
Salt Bridges ◽  
Histidine Residues ◽  
Human Prolactin

AbstractExperimental data shows that the binding of human prolactin (hPRL) to human prolactin receptor (hPRLr-ECD) is strongly pH-dependent, while the binding of the same receptor to human growth hormone (hGH) is pH-independent. Here we carry in silico analysis of the molecular effects causing such a difference and reveal the role of individual amino acids. It is shown that the computational modeling correctly predicts experimentally determined pKa’s of histidine residues in an unbound state in the majority of the cases and the pH-dependence of the binding free energy. Structural analysis carried in conjunction with calculated pH-dependence of the binding revealed that the main reason for pH-dependence of the binding of hPRL-hPRLr-ECD is a number of salt-bridges across the interface of the complex, while no salt-bridges are formed in the hGH-hPRlr-ECD. Specifically, most of the salt-bridges involve histidine residues and this is the reason for the pH-dependence across a physiological range of pH. The analysis not only revealed the molecular mechanism of the pH-dependence of the hPRL-hPRLr-ECD, but also provided critical insight into the underlying physic-chemical mechanism.

Determination of antibodies against human growth hormone using a direct immunoassay format and different electrochemical methods

The Analyst ◽  
2013 ◽  
Vol 138 (5) ◽  
pp. 1427 ◽  
Author(s):  
Natalija German ◽  
Asta Kausaite-Minkstimiene ◽  
Justina Kirlyte ◽  
Asta Makaraviciute ◽  
Arunas Ramanavicius ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Electrochemical Methods ◽  
Direct Immunoassay
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