Interaction of molybdenum with human erythrocyte membrane proteins
| Autor: | B. Bíbr, Jaroslav Lener, Tomáš Mařík, Marie Kselíková |
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| Rok vydání: | 1979 |
| Předmět: |
Chromatography
Endocrinology Diabetes and Metabolism Biochemistry (medical) Clinical Biochemistry Peripheral membrane protein chemistry.chemical_element General Medicine Ascorbic acid Biochemistry Inorganic Chemistry chemistry.chemical_compound Membrane chemistry Molybdenum Spectrin Hemoglobin Sodium dodecyl sulfate Polyacrylamide gel electrophoresis |
| Zdroj: | Biological trace element research. 2(1) |
| ISSN: | 0163-4984 |
| Popis: | This study describes the interaction of molybdenum with blood components. Molybdenum-99 was added to blood, and after four washings, 3% of the total radioactivity was found in red cells. More specifically, the radioactivity was determined to be associated with the cell membrane.Molybdenum-99 in the +VI form did not interact with the human erythrocyte membrane; however, Mo(V) forms did interact. Of five different compounds, the highes uptake was observed with a brown Mo(V)-ascorbate complex generated from Mo(VI) and ascorbic acid in the molar ratio 1∶20. A membrane suspension of Mo-ascorbate-treated human erythrocytes was prepared and the solubilized proteins were separated on a polyacrylamide gel in the presence of sodium dodecyl sulfate (SDS). Molybdenum-99 binding to spectrin was demonstrated, as well as some minor interactions with membrane hemoglobin and bands 6 and 8. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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