Chelation of mercury by ouabain-sensitive and ouabain-resistant renal Na,K-ATPase
| Autor: | E. Imesch, Beatrice M. Anner, M. Moosmayer |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
medicine.medical_treatment
Biophysics chemistry.chemical_element Biochemistry Ouabain chemistry.chemical_compound medicine Animals Chelation Cysteine Na+/K+-ATPase Antidote Molecular Biology Edetic Acid Kidney Medulla Dimercaprol Dithiol Cell Biology Rats Mercury (element) Kinetics chemistry Mercuric Chloride Rabbits Sodium-Potassium-Exchanging ATPase Protein Binding medicine.drug |
| Zdroj: | Biochemical and Biophysical Research Communications. 167:1115-1121 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(90)90638-4 |
| Popis: | The SH-reactive HgCl2 inhibits the Na,K-ATPase activity potently in a manner antagonized only partially by EDTA or cysteine; solely dimercaprol, a dithiol antidote for mercury, blocks the HgCl2 effects entirely as confirmed also by 203Hg-binding experiments. The results reveal the presence of a chelating component in pure Na,K-ATPase with an affinity for mercury superior to EDTA. The mercury-sensitivity of the Na,K-ATPase is not related to the ouabain-sensitivity. This criterion will be useful for the distinction between ouabain-like and mercury-like inhibitors from body fluids and tissues. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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