scholarly journals Solid-Phase Radioimmunoassay of Human Growth Hormone

1966 ◽  
Vol 100 (3) ◽  
pp. 31C-33C ◽  
Author(s):  
Kevin Catt ◽  
H. D. Niall ◽  
G. W. Tregear
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Solid Phase ◽  
Human Growth ◽  
Solid Phase Radioimmunoassay

Solid-phase radioimmunoassay for human growth hormone

1969 ◽  
Vol 6 (5) ◽  
pp. 699-713 ◽  
Author(s):  
J.B. Baumann ◽  
J. Girard ◽  
M. Vest
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Solid Phase ◽  
Human Growth ◽  
Solid Phase Radioimmunoassay

scholarly journals Molecular and cellular actions of a structural domain of human growth hormone (AOD9401) on lipid metabolism in Zucker fatty rats

2000 ◽  
Vol 25 (3) ◽  
pp. 287-298 ◽  
Author(s):  
FM Ng ◽  
WJ Jiang ◽  
R Gianello ◽  
S Pitt ◽  
P Roupas
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Chronic Treatment ◽  
Solid Phase ◽  
Human Growth ◽  
The Body ◽  
Laboratory Animals ◽  
Zucker Rats ◽  
Structural Domain ◽  
Average Cell

A lipolytic domain (AOD9401) of human growth hormone (hGH) which resides in the carboxyl terminus of the molecule and contains the amino acid residues 177-191, has been synthesized using solid-phase peptide synthesis techniques. AOD9401 stimulated hormone-sensitive lipase and inhibited acetyl coenzyme A carboxylase (acetyl CoA carboxylase) in isolated rat adipose tissues, in a similar manner to the actions of the intact hGH molecule. The synthetic lipolytic domain mimicked the effect of the intact growth hormone on diacylglycerol release in adipocytes. Chronic treatment of obese Zucker rats with AOD9401 for 20 days reduced the body weight gain of the animals, and the average cell size of the adipocytes of the treated animals decreased from 110 to 80 microm in diameter. Unlike hGH, synthetic AOD9401 did not induce insulin resistance or glucose intolerance in the laboratory animals after chronic treatment. The results suggest that AOD9401 has the potential to be developed into a therapeutic agent for the control of obesity.

Modified solid-phase (tube) radioimmunoassay of human growth hormone

1969 ◽  
Vol 47 (9) ◽  
pp. 803-814
Author(s):  
R. M. Bala ◽  
K. A. Ferguson ◽  
J. C. Beck
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Protein Concentration ◽  
Solid Phase ◽  
Ionic Composition ◽  
Rabbit Antiserum ◽  
Human Growth ◽  
Phase System ◽  
Nonspecific Binding ◽  
Free Antibody

Polystyrene tubes were coated with rabbit antiserum to human growth hormone (HGH). Bovine serum albumin (BSA) in buffer, HGH standard or unknown samples, and 125I-HGH were added to the antibodycoated tubes. After incubation the radioactivity in each tube was counted, the incubate discarded, the tubes were washed, and radioactivity was recounted. The sensitivity of the assay was consistently 0.05 mμg HGH or less. Nonspecific binding by uncoated tubes was less than 1%. It was preferable to control the surface area exposed to excess antiserum rather than limit the concentration of the antiserum. Polypropylene and polystyrene tubes gave similar results. Variation of ionic composition or pH of the incubate had no significant effects. Maximum precision and sensitivity occurred with incubation at 4 °C for 40 to 60 h. Addition of posthypophysectomy human plasma or varying the protein concentration had similar effects. The immobilized antibody may be more selective in binding with antigen than is free antibody in solution. Our modifications combine favorable features of the solid-phase system with an increase in sensitivity and greater economy of materials.

A thiol functionalized cryogel as a solid phase for selective reduction of a cysteine residue in a recombinant human growth hormone variant

2014 ◽  
Vol 173 ◽  
pp. 76-85 ◽  
Author(s):  
Gry Ravn Jespersen ◽  
Finn Matthiesen ◽  
Anja Kallesøe Pedersen ◽  
Henrik Sune Andersen ◽  
Harald Kirsebom ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Solid Phase ◽  
Recombinant Human Growth Hormone ◽  
Selective Reduction ◽  
Human Growth ◽  
Cysteine Residue
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