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- W1994476265 abstract "Contamination with hemoglobin in human liver mitochondria prepared by the procedure commonly applied to rat liver is unavoidable and a major obstacle to the measurement of cytochromes by (reduced minus oxidized) difference spectra. The washing of sliced liver tissues with Lock's solution minimized the contamination with hemoglobin. A systematic method has been presented for quantitatively estimating the respiratory pigments without complete removal of hemoglobin. Phosphorylative activity and respiratory enzyme contents were assayed in the mitochondria prepared from 67 biopsy specimens of normal human liver obtained at operation. The maximal phosphorylation rates were 41.7 nmoles ATP synthesis per mg protein per min at 22° with glutamate plus succinate as substrates (on a protein basis) and 36.6 per second (on a cytochrome a(+a3) basis, “cytochrome a(+a3)-turnover”). No statistically significant decline in the phosphorylation rates with increasing age could be demonstrated. The cytochrome a(+a3) concentration was fairly constant during the life span, while there was a significant elevation of cytochrome c + c1 concentration with increasing age. After 70 years of age the cytochrome c + c1 level increased 1.6-fold, from 76 to 121 pmoles per mg of mitochondrial protein, as compared with young adults. In the young adult cytochrome c + c1 concentration did not exceed that of cytochrome a(+a3). The ratio of cytochrome c + c1 to cytochrome a(+a3) increased after 60 years of age, and cytochrome c + c1 concentration was 1.5 times higher than the cytochrome a(+a3) concentration after 70 years of age." @default.
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- W1994476265 date "1972-05-01" @default.
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- W1994476265 title "Human liver mitochondria" @default.
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- W1994476265 doi "https://doi.org/10.1016/0009-8981(72)90130-1" @default.
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