Influence of divalent cations on the detection of somatogenic and lactogenic binding sites in mouse liver cells
| Autor: | J M Dellacha, G N Ciccia-Torres |
|---|---|
| Rok vydání: | 1985 |
| Předmět: |
Male
animal structures Cations Divalent Receptors Prolactin Ratón Cell chemistry.chemical_element Male mice Receptors Cell Surface Calcium Binding Competitive Biochemistry Divalent Mice medicine Animals Binding site Molecular Biology Edetic Acid chemistry.chemical_classification Binding Sites Receptors Somatotropin Cell Biology Prolactin medicine.anatomical_structure Liver chemistry Growth Hormone Hepatocyte hormones hormone substitutes and hormone antagonists Research Article |
| Zdroj: | Biochemical Journal. 228:761-764 |
| ISSN: | 1470-8728 0264-6021 |
| DOI: | 10.1042/bj2280761 |
| Popis: | Specific binding of 125I-labelled human somatotropin was demonstrated in isolated hepatocytes from male mice. In the presence of divalent cations (Ca2+ and Mg2+) the binding of 125I-labelled human somatotropin was competitive with ovine prolactin. Scatchard analysis of competition data indicated a KD of 1.4 +/- 0.2 nM and a binding capacity of 13 000 +/- 2000 sites/cell. In the absence of divalent cations and in the presence of EDTA, human and bovine somatotropins were found to be equally effective to displace bound 125I-labelled human somatotropin, while ovine prolactin showed a weak competition. In this case, the binding capacity was 8400 +/- 1500 sites/cell and the KD was 1.1 +/- 0.1 nM. |
| Databáze: | OpenAIRE |
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