Ligand Binding in Allosteric Flavoproteins: Part 1. Quantitative Analysis of the Interaction with NAD+ of the Apoptosis Inducing Factor (AIF) Harboring FAD in the Reduced State
| Autor: | Cocomazzi P., Sorrentino L., Cossu F., Aliverti A. |
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| Jazyk: | angličtina |
| Rok vydání: | 2021 |
| Předmět: | |
| Zdroj: | Methods in molecular biology (Clifton N.J., Online) 2280 (2021): 179–187. doi:10.1007/978-1-0716-1286-6_11 info:cnr-pdr/source/autori:Cocomazzi P.; Sorrentino L.; Cossu F.; Aliverti A./titolo:Ligand Binding in Allosteric Flavoproteins: Part 1. Quantitative Analysis of the Interaction with NAD+ of the Apoptosis Inducing Factor (AIF) Harboring FAD in the Reduced State/doi:10.1007%2F978-1-0716-1286-6_11/rivista:Methods in molecular biology (Clifton N.J., Online)/anno:2021/pagina_da:179/pagina_a:187/intervallo_pagine:179–187/volume:2280 |
| Popis: | To perform their action, flavoproteins usually interact with a variety of low molecular weight partners, including electron transporters, yielding transient complexes whose tightness is often controlled by the redox state of the bound flavin cofactor. As a case study, here we describe the quantitative analysis of the redox-dependent interaction of the mammalian apoptosis inducing factor (AIF) with its NAD+ ligand. In particular, we report a protocol for the spectrophotometric titration of AIF in its reduced state under anaerobic conditions with NAD+, in order to determine the dissociation constant of the resulting complex. © 2021, Springer Science+Business Media, LLC, part of Springer Nature. |
| Databáze: | OpenAIRE |
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