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. 1988 Apr 15;251(2):385–389. doi: 10.1042/bj2510385

A study of GDP binding to purified thermogenin protein from brown adipose tissue.

R R French 1, M G Gore 1, D A York 1
PMCID: PMC1149014  PMID: 3135798

Abstract

1. The binding of GDP to purified thermogenin protein was studied by using fluorescence spectroscopy and equilibrium dialysis. 2. GDP binding to thermogenin diminished fluorescence emission in a concentration-dependent manner that exhibited saturation. 3. Kd values for binding of nucleoside di- and tri-phosphates were lower than those for nucleoside monophosphates. 4. The GDP-induced fluorescence quenching was decreased by increasing pH, but the apparent Kd was unaltered by pH changes. 5. Equilibrium dialysis showed a Kd change from 3 to 6 microM when the pH was increased from 6.6 to 8.5. 6. The apparent pK of the fluorescence changes induced by pH (8.3) was identical with the apparent pK of the GDP-binding response. 7. The data are consistent with the existence of protonated and non-protonated forms of thermogenin protein that both bind GDP.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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