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- W1489506779 abstract "Cytochrome b was purified from Neurospora crassa mitochondria by means of chromatography on oleyl-polymethacrylic acid resin, chromatography on DEAE-cellulose and recycling gel filtration on Sephadex G-75, all steps being performed in a medium containing bile acids and salts. The heme content of the preparation was calculated on the basis of incorporated 59Fe and [3H]-leucine to be 33–40 μmol/g protein, corresponding to a minimum molecular weight of 25000 to 30000. Upon gel filtration on Sephadex G-75 in a bile acid and KCl medium the preparation migrated like a 55000-molecular-weight protein. Upon gel electrophoresis on polyacrylamide or upon gel filtration on Sephadex G-100 in a dodecylsulfate medium the protein part of the preparation migrated as one band of the apparent molecular weight of approximately 30000. These findings suggest that the purified cytochrome b is a dimeric heme protein. In vivo incorporation of [3H]leucine into the protein part of the purified cytochrome b was insensitive to cycloheximide but sensitive to chloramphenicol. This indicates that the apoprotein of cytochrome b is translated on mitochondrial ribosomes." @default.
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- W1489506779 date "1974-01-01" @default.
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- W1489506779 title "Cytochrome b in Neurospora crassa Mitochondria. Site of Translation of the Heme Protein" @default.
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- W1489506779 doi "https://doi.org/10.1111/j.1432-1033.1974.tb03244.x" @default.
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