| Autor: |
Martinis, Pamela, Battaglia, Valentina, Grancara, Silvia, Dalla Via, Lisa, Di Noto, Vito, Saccoccio, Stefania, Agostinelli, Enzo, Bragadin, Marcantonio, Grillo, Maria, Toninello, Antonio |
| Předmět: |
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| Zdroj: |
Amino Acids; Feb2012, Vol. 42 Issue 2/3, p761-768, 8p |
| Abstrakt: |
Agmatine, a divalent diamine with two positive charges at physiological pH, is transported into the matrix of liver mitochondria by an energy-dependent mechanism, the driving force of which is the electrical membrane potential. Its binding to mitochondrial membranes is studied by applying a thermodynamic treatment of ligand-receptor interactions on the analyses of Scatchard and Hill. The presence of two mono-coordinated binding sites S and S, with a negative influence of S on S, has been demonstrated. The calculated binding energy is characteristic for weak interactions. S exhibits a lower binding capacity and higher binding affinity both of about two orders of magnitude than S. Experiments with idazoxan, a ligand of the mitochondrial imidazoline receptor I, demonstrate that S site is localized on this receptor while S is localized on the transport system. S would act as a sensor of exogenous agmatine concentration, thus modulating the transport of the amine by its binding to S. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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