CHARACTER OF STORED MOLECULES IN CHROMAFFIN GRANULES OF ADRENAL-MEDULLA - NUCLEAR MAGNETIC-RESONANCE STUDY

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1978
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The organization of the internal contents of bovine adrenal chromaffin granules were studied using NMR spectroscopy. The method permits an examination of the interactions between ATP metal ions, adrenaline [epinephrine] and the chromogranin proteins. Particular advantage accrues when the naturally occurring cations Mg and Ca are replaced by Mn cations, since Mn2+ is an effective perturbing probe. Protein spectrum in the vesicles was compared with that of the isolated proteins. There was a loose network of interactions between the various components. The major part of the network was the interaction of the chromogranin protein, shown to have approximately a random coil conformation, with the ATP and the adrenaline. The organized loose structure appeared to lower osmotic pressure without hindering rapid release of the vesicle contents breaking the membrane.
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