-transparent.png){kind=logo}
The biosynthesis of pyridine dinucleotide transhydrogenase has been studied in isolated rat hepatocytes and in a rabbit reticulocyte-lysate translation system supplemented with either intact isolated rat liver mitochondria or the soluble matrix fraction from isolated mitochondria. In intact hepatocytes, the transhydrogenase precursor was short-lived in the cytosol and was efficiently imported into the membranous fraction. When the cell-free translation mixture was incubated with intact mitochondria, the transhydrogenase precursor was processed to the mature form, to an extent that depended on the amount of added mitochondria. Incubation of the translation mixture with the soluble mitochondria matrix fraction converted the precursor to a mature-sized protein with 75% efficiency, this being blocked by various proteinase inhibitors such as EDTA, 1,10-phenanthroline and leupeptin.
L N Wu, and
I M Lubin, and
R R Fisher
September 1987,
Archives of biochemistry and biophysics,
L N Wu, and
I M Lubin, and
R R Fisher
November 1982,
Biochemical pharmacology,
L N Wu, and
I M Lubin, and
R R Fisher
December 1994,
DNA and cell biology,
L N Wu, and
I M Lubin, and
R R Fisher
November 1984,
The Journal of biological chemistry,
L N Wu, and
I M Lubin, and
R R Fisher
September 2003,
Nucleic acids research,
L N Wu, and
I M Lubin, and
R R Fisher
July 1997,
The Journal of biological chemistry,
L N Wu, and
I M Lubin, and
R R Fisher
September 1981,
Biochemical and biophysical research communications,
L N Wu, and
I M Lubin, and
R R Fisher
February 1960,
Biochimica et biophysica acta,
L N Wu, and
I M Lubin, and
R R Fisher
July 1983,
Biochimica et biophysica acta,
L N Wu, and
I M Lubin, and
R R Fisher
September 1976,
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.),
