Properties of a Chromoprotein Containing Extract of the Particulate Fraction of Rat Liver

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Abstract
An extract of washed rat liver particles (mitochondria) was prepared by treating a suspension of the particulate fraction of KCl (0.15 [image]) homogenates with ice-cold isobutanol in presence of phosphate buffer and a dilute soln. of Na carboxymethylcellulose as protective colloid. After removal of the isobutanol, either by dialysis or by freeze-drying, a flavoprotein-heme-protein-containing soln. was obtained, which reduced cytochrome c if reduced co-enzyme I or II was added to the system. The enzymatic properties of the extract were measured spectrophotometrically. The oxidized flavoprotein had absorption maxima at 450 and 469 m[mu], the oxidized heme-protein a Soret band at 415 m[mu]. Upon reduction with hydrosulfite the flavin maxima disappeared, while a shift in the Soret region to 430 mu occurred and peaks at 530 and 560 m[mu] appeared. The heme-protein (cytochrome B) was reduced enzy-matically by yeast alcohol dehydrogenase and Zwischenferment. The extract contained peroxidase and also nucleotidase.