In vivo bioassay for the potency determination of human growth hormone in dwarf "little" mice.

Endocrinology ◽  
1993 ◽  
Vol 132 (5) ◽  
pp. 2051-2055 ◽  
Author(s):  
M H Bellini ◽  
P Bartolini
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
In Vivo Bioassay

A new bioassay for human growth hormone based on incorporation of labelled proline into skin

1982 ◽  
Vol 95 (1) ◽  
pp. 81-86 ◽  
Author(s):  
C. G. Rudman ◽  
Rose E. Gaines Das ◽  
J. A. Parsons
Keyword(s):  
Growth Hormone ◽  
Weight Gain ◽  
Human Growth Hormone ◽  
Dose Response ◽  
Human Growth ◽  
Hypophysectomized Rats ◽  
In Vivo Bioassay ◽  
New Bioassay ◽  
Average Index

An in-vivo bioassay for human growth hormone (hGH) has been developed, based on the dose-related enhancement of radioactivity in skin of hypophysectomized rats given daily s.c. injections of hGH and a single i.p. injection of labelled proline. The measured radioactivity, taken as the response, was shown to be independent of the site at which the skin was sampled. Valid dose–response relationships were obtained after as little as 3 days of treatment with GH. The assays by this method are shown to be more precise than the widely used weight-gain and tibial-width bioassays. Assays carried out gave an average index of precision of 0·036.

Reduced and S-carboxymethylated human growth hormone: a probe for diabetogenic action

1984 ◽  
Vol 247 (5) ◽  
pp. E639-E644
Author(s):  
C. M. Cameron ◽  
J. L. Kostyo ◽  
J. A. Rillema ◽  
S. E. Gennick
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Mouse Mammary Gland ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Hypophysectomized Rats

The biological activity profile of reduced and S-carboxymethylated human growth hormone (RCM-hGH) was determined to establish its suitability for study of the diabetogenic property of hGH. RCM-hGH was found to have greatly attenuated in vivo growth-promoting activity in the 9-day weight-gain test in hypophysectomized rats (approximately 1%) and to have a similar low order of in vitro activity in stimulating amino acid incorporation into the protein of the isolated rat diaphragm. RCM-hGH also only had approximately 1% of the in vitro insulin-like activity of the native hormone on isolated adipose tissue from hypophysectomized rats. In contrast, RCM-hGH retained substantial in vivo diabetogenic activity in the ob/ob mouse, appearing to have approximately 50% of the activity of the native hormone. RCM-hGH was also found to retain significant, although attenuated (25%), in vitro lactogenic activity when tested for the ability to stimulate amino acid incorporation into a casein-rich protein fraction in mouse mammary gland explants. Because RCM-hGH exhibits a high degree of diabetogenic activity, although lacking significant anabolic or insulin-like activities, it will be useful as a "monovalent" probe for the study of the molecular mechanism of the diabetogenic action of GH.

Design and in vivo evaluation of solid-in-oil suspension for oral delivery of human growth hormone

2008 ◽  
Vol 41 (2) ◽  
pp. 106-110 ◽  
Author(s):  
Hiromu Yoshiura ◽  
Yoshiro Tahara ◽  
Masakazu Hashida ◽  
Noriho Kamiya ◽  
Akihiko Hirata ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Oral Delivery ◽  
Human Growth ◽  
In Vivo Evaluation

New Gaba-containing analogues of human Growth Hormone Releasing Hormene (1–30)-amide: II. Detailed in vivo biological examinations

1993 ◽  
Vol 16 (10) ◽  
pp. 799-805 ◽  
Author(s):  
Magdolna Kovàcs ◽  
I. Mezõ ◽  
I. Teplán ◽  
M. Hollósi ◽  
J. Kajtár ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth

Nasal delivery of human growth hormone: in vitro and in vivo evaluation of a thiomer/glutathione microparticulate delivery system

2004 ◽  
Vol 100 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Verena M. Leitner ◽  
Davide Guggi ◽  
Alexander H. Krauland ◽  
Andreas Bernkop-Schnürch
Keyword(s):  
Growth Hormone ◽  
Delivery System ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Nasal Delivery ◽  
In Vivo Evaluation

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.

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