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• W1510123264 abstract "Abstract Fractionation studies of rat liver have shown that the mitochondria thereof contain more than 90% of the total cytochrome c of the tissue upon their isolation. Reproducible small complements of the remainder of the cytochrome c were found in each of other cell fractions. The intracellular site of synthesis of cytochrome c was determined by use of 3 H-δ-aminolevulinic acid ( 3 H-ALA) as a precursor of hematoheme. In short intervals of labeling following intraperitoneal injection of 3 H-ALA into mature rats, the specific activity of the hematoheme of microsomal cytochrome c greatly exceeded that of mitochondrial cytochrome c ; after 2 hr of incorporation, the two specific activities approached a common value. When short intervals were employed for incorporation of 3 H-ALA, followed by an additional interval in the presence of a molar excess of ALA it, was possible to show a precursor-product relationship between the respective microsomal and mitochondrial complements of cytochrome c . The findings indicate that the endoplasmic reticulum catalyzes the complete assembly of cytochrome c whereupon the completed protein is then transferred to the mitochondria." @default.
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• W1510123264 date "1969-09-01" @default.
• W1510123264 modified "2023-09-25" @default.
• W1510123264 title "Origin of mitochondrial enzymes" @default.
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• W1510123264 doi "https://doi.org/10.1016/0003-9861(69)90463-9" @default.
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