Abstract
C. F. Strittmatter and Ball1 have localized a hæm protein in liver microsomes which they have termed ‘cytochrome m’ This hæmochromogen was first studied by Keilin and Hartree2 in liver homogenates and was termed by them cytochrome b 1. Pappenheimer and Williams3, who studied this pigment in the Cecropia larvæ, have designated it ‘cytochrome b 5’. P. Strittmatter and Velick4 have isolated this cytochrome from rabbit liver microsomes and studied its properties. These workers5 have also prepared a reduced diphosphopyridine nucleotide–microsomal cytochrome reductase from the same cellular material. This reductase is totally inactive with cytochrome c but catalyses the transfer of electrons from reduced diphosphopyridine nucleotide to the microsomal cytochrome. The microsomal cytochrome transfers electrons directly to cytochrome c. Thus, cytochrome m completes a reduced diphosphopyridine nucleotide–cytochrome c reductase system which involves an electron transfer from cytochrome to cytochrome.
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References
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SHULL, K. A Microsomal Malic Dehydrogenase. Nature 183, 259–260 (1959). https://doi.org/10.1038/183259a0
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DOI: https://doi.org/10.1038/183259a0
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