1986
DOI: 10.1111/j.1399-3011.1986.tb03228.x
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Structure‐function studies on human growth hormone

Abstract: The relationship between the conformation of human pituitary growth hormone (hGH), biological activity, and ligand binding activity was studied by comparing conformational details previously published on in vivo and in vitro studies of identical samples of hGH and its known derivatives. In vivo assays included the rat tibia test for somatotropic activity and the pigeon crop‐sac assay for lactogenic hormone activity. Relative binding affinities were compared in radioimmuno‐assays using 125I‐hGH as tracer with 1… Show more

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Cited by 10 publications
(2 citation statements)
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“…They selectively reduced and alkylated either both GH disulphide bonds or only the C-terminal one. C-terminally carboxymethylated GH showed the same biological activity in rat tibia and pigeon crop sac tests as unaltered GH, whereas the fully carboxymethylated GH displayed decreased activity in both tests -in accordance with the studies using CXY-GH described above [23,25,26].…”
Section: Early Researchsupporting
confidence: 70%
See 1 more Smart Citation
“…They selectively reduced and alkylated either both GH disulphide bonds or only the C-terminal one. C-terminally carboxymethylated GH showed the same biological activity in rat tibia and pigeon crop sac tests as unaltered GH, whereas the fully carboxymethylated GH displayed decreased activity in both tests -in accordance with the studies using CXY-GH described above [23,25,26].…”
Section: Early Researchsupporting
confidence: 70%
“…However, their conformation did not differ from unmodified GH when analysed by circular dichroism spectrum [25].…”
Section: Early Researchmentioning
confidence: 99%