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説明
Two cytochrome b preparations have been prepared from Complex III of beef heart mitochondria, by detergent-exchange chromatography on a butyl-Toyopearl column. One was eluted from the column with buffer containing Tween 20 after most of other subunits of Complex III were eluted with buffer containing guanidine-HCl, and the other was eluted from the column with buffer containing sodium dodecyl sulfate. The former is consisted of a single polypeptide (subunit III) and contained 37.5 nmol of heme b/mg of protein, and the latter consisted of subunits III and IX and contained 19.5 nmol of heme b/mg of protein. The former was labile when it was reduced by dithionite, whereas the latter was stable. Subunit IX in the latter is associated with cytochrome b even after gel filtration and density gradient centrifugation. These results suggest that subunit IX plays a role in stabilizing cytochrome b.
収録刊行物
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- Biochemical and Biophysical Research Communications
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Biochemical and Biophysical Research Communications 132 1166-1173, 1985-11-01
Elsevier BV