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. 1983 Feb 1;209(2):541-5.
doi: 10.1042/bj2090541.

Electron transfer flavoprotein from pig liver mitochondria. A simple purification and re-evaluation of some of the molecular properties

M Husain, D J Steenkamp

Electron transfer flavoprotein from pig liver mitochondria. A simple purification and re-evaluation of some of the molecular properties

M Husain et al. Biochem J. .

Abstract

Electron transfer flavoprotein (ETF) from pig liver mitochondria has been purified to homogeneity by a three-step procedure with approx. 10-fold higher yields than previously reported. The purified ETF exhibits an absorption coefficient for the bound FAD of 13.5 mM-1.cm-1 at 436 nm and an isoelectric point of 6.75. Gel filtration, sodium dodecyl sulphate gel electrophoresis and flavin analysis indicate that pig liver ETF is a dimer, composed of non-identical subunits (Mr 38 000 and 32 000) with only one FAD/dimer. Anaerobic reduction by dithionite produces anionic flavin semiquinone as a stable intermediate and establishes the flavin to be the only redox-active chromophore in ETF.

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