Changes in GDP binding to brown adipose tissue mitochondria and the uncoupling protein
| Autor: | A. G. Swick, R. W. Swick |
|---|---|
| Rok vydání: | 1988 |
| Předmět: |
Male
Physiology Acclimatization Endocrinology Diabetes and Metabolism Phosphatase Adipose tissue Guanosine Diphosphate Ion Channels Divalent Mitochondrial Proteins chemistry.chemical_compound Adipose Tissue Brown Physiology (medical) Brown adipose tissue medicine Animals Uncoupling protein Magnesium Binding site Uncoupling Protein 1 chemistry.chemical_classification Chemistry GDP binding Membrane Proteins Rats Inbred Strains Alkaline Phosphatase Guanine Nucleotides Mitochondria Rats Cold Temperature medicine.anatomical_structure Biochemistry Guanosine diphosphate Calcium Spermine Carrier Proteins |
| Zdroj: | American Journal of Physiology-Endocrinology and Metabolism. 255:E865-E870 |
| ISSN: | 1522-1555 0193-1849 |
| DOI: | 10.1152/ajpendo.1988.255.6.e865 |
| Popis: | Incubation in vitro of brown adipose tissue (BAT) mitochondria with divalent cations, spermine, or alkaline phosphatase led to a marked increase in the binding of [3H]GDP. The effect of Mg2+ appeared to be the most specific and led to the largest increase in GDP binding. A simplified method was developed for measuring GDP binding to purified uncoupling protein from rat BAT mitochondria. Application of this method indicates that uncoupling protein from cold-acclimated rats binds twice as much GDP as uncoupling protein from cold-acclimated rats that were briefly returned to thermoneutrality, paralleling changes in GDP binding to the mitochondria. Incubation of BAT mitochondria with Mg2+ led to a smaller increase in GDP binding to the subsequently purified uncoupling protein, suggesting that divalent cations may somehow participate in the regulation of the activity of the uncoupling protein. |
| Databáze: | OpenAIRE |
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