Growth Hormone Radioligand Assay Unresponsive to Human Prolactin

Etzrodt, H.; Musch, K.; Schleyer, M.; Pfeiffer, E. F.

doi:10.1210/jcem-42-6-1184

Cited by 12 publications

(7 citation statements)

References 6 publications

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“…Rabbit and rat liver plasma membranes contain high affinity receptors for hGH (Moore and Jin 1978;Posner, Kelly and Friesen 1974;Etzrodt, Musch and Schleyer 1976;Ranke, Stanley, Tenore, Rodbard, Bongiovanni and Parks 1976;Hughes 1979). The receptors for hGH on female rat liver membranes are termed lactogenic in nature as determined by competitive binding of lactogenic hormone such as oPrl.…”

Section: Discussionmentioning

confidence: 99%

Binding of a Variant of Human Growth Hormone to Liver Plasma Membranes

Wohnlich¹,

Moore²

1982

Horm Metab Res

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The binding of human growth hormone (hGH) and a naturally occurring variant of hGH (20K) to rat and rabbit liver membrane has been compared. The concentration of hormone causing half maximal displacement (ED50) of 125I-hGH from rat liver plasma membranes was 1.6 nM for hGH and 46 nM for 20K. The ED50 for hGH and 20 K against 125I-hGH binding to rabbit liver plasma membranes was 1.6 mM for hGH and 28 nM for 20K. Significant binding of 125I-20K did occur to rat and rabbit liver membranes but the relative capacities for 20K were 12 and 6 fold less in rat and rabbit liver membranes, respectively when compared to hGH. The competitive binding characteristics of 20K to pregnant rabbit liver membranes indicated lack of competition between bovine GH and 125I-20K for binding. However, significant binding of 125I-20K to male rabbit liver membranes was present and displaceable by hGH and oPrl. We conclude that deletion of a portion of the hGH molecule (defined as residues 32-46) results in significant alterations in the binding characteristics of the molecule. This indicates primary or secondary involvement of this portion of the hGH molecules in the binding process and may define a portion of the binding domain for hGH.

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Section: Discussionmentioning

confidence: 99%

Binding of a Variant of Human Growth Hormone to Liver Plasma Membranes

Wohnlich¹,

Moore²

1982

Horm Metab Res

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“…Female rat hepatocytes display both kinds of receptors (Ranke et al, 1976a,b;Postel-Vinay & Desbuquois, 1977), but other biological preparations have only one of them. Thus in hepatocytes from male rats (Ranke et al, 1976a,b;Postel-Vinay & Desbuquois, 1977) or hypophysectomized rats (Turyn et al, 1976), in liver microsomal fraction ('microsomes') from male rats (Postel-Vinay, 1976) and in plasma membranes from female rats (Etzrodt et al, 1976), only somatogenic receptors are found.…”

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confidence: 99%

Characterization of human somatotropin binding to detergent-solubilized lactogenic receptors from rat liver

Bonifacino¹,

Sánchez²,

Paladini³

1981

Biochemical Journal

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Lactogenic receptors from rat liver microsomal fraction ('microsomes') were extracted by treatment with 1% (w/v) Triton X-100. Triton X-100 exerts an inhibitory effect on both the binding reaction and the separation of the free hormone from the complex. The association and dissociation of 125I-labelled human somatotropin are time- and temperature-dependent processes. The association rate constant, k1, is 6.7 x 10(6) mol . litre-1 . min-1 at 25 decrees C, and the dissociation rate constant, k-1, is 1.1 x 10(-3) min-1 at 25 degrees C. Scatchard analysis of saturation data reveals the existence of a single class of receptors and that solubilization leads to a slight decrease in affinity and a sharp increase in binding capacity. The dissociation constant, Kd, of the solubilized preparation is 0.22 nM and the binding capacity 2900 fmol/mg of protein. Similar results were obtained from competition experiments. Binding of 125I-labelled human somatotropin to the solubilized receptors is specifically inhibited by hormones with lactogenic activity. Incubation of the solubilized preparation with trypsin resulted in an 80% decrease in binding activity. The solubilized form of the receptor has a slightly increased sensitivity to the inactivation by trypsin, heat and extremes of pH, with respect to the membrane-bound form.

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“…Growth hormone activity in vivo was determined by a modified tibia test' l°L Furthermore, the activity of the hormone was tested by a radioligand assay' 11 …”

Section: Measurements Of Hormone Activitiesmentioning

confidence: 99%

Preparation of Highly Purified Human Somatotropin (Growth Hormone)

Schleyer¹,

Voigt²

1977

Hoppe-Seyler´s Zeitschrift für physiologische Chemie

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A method for preparation of highly purified human somatotropin on large-scale basis is described. Starting from deep-frozen pituitary glands, less time is needed to obtain highly purified hormone than with other published methods for preparation of human somatotropin. The hormone obtained in this fashion is chromatographically and electrophoretically homogeneous; it shows high biological and radioimmunological growth hormone activity and is free of other pituitary hormone activities. The effects of various experimental conditions upon aggregation of somatotropin are critically evaluated. Darstellung von hochgereinigtem humanem Somatotropin (Wachstumshormon)Zusammenfassung: Es wird eine Methode zur Herstellung von hochgereinigtem humanem Somatotropin in präparativem Maßstab beschrieben. Zur Gewinnung des hochgereinigten Hormons aus tiefgefrorenen Hypophysen wird nach diesem Verfahren weniger Zeit benötigt als nach anderen zur Herstellung von Somatotropin beschriebenen Methoden. Das erhaltene Hormon ist chromatographisch und elektrophoretisch einheitlich, zeigt hohe biologische und radioimmunologische Aktivität und ist frei von Aktivitäten anderer hypophysärer Hormone. Der Einfluß angewandter experimenteller Bedingungen auf die Tendenz des Somatotropins, Aggregate zu bilden, wird diskutiert.

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Growth Hormone Radioligand Assay Unresponsive to Human Prolactin

Cited by 12 publications

References 6 publications

Binding of a Variant of Human Growth Hormone to Liver Plasma Membranes

Binding of a Variant of Human Growth Hormone to Liver Plasma Membranes

Characterization of human somatotropin binding to detergent-solubilized lactogenic receptors from rat liver

Preparation of Highly Purified Human Somatotropin (Growth Hormone)

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