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- W2037741154 abstract "Mitochondrial and lysosome membrane permeability has been studied in terms of changes in structure-linked enzyme activity. A linear correlation of particle light scattering and mitochondrial dehydrogenase activation was obtained as a function of Cu2+-induced volume change. Mitochondrial dehydrogenase and lysosome hydrolase activities varied in accord with Boyle-van't Hoff's laws suggesting that both particle systems behave as osmometers in KCl solutions. The rate of permeation of a solute into mitochondria or lysosomes was obtained from the rates of enzyme activation in isosmolar solute. Mitochondria and lysosomes were permeable to ammonium, acetate, and phosphate ions. Electron microscopy of mitochondrial pellets prepared by centrifugation after preincubation in isosmolar glycerol or ammonium phosphate revealed mitochondrial changes consisting of a condensed → swollen conformation. Glycerol induced a loss of lysosome matrix but only partial lysosome destruction was seen after preincubation in ammonium phosphate. Such semiquantitative analyses of lysosomevacuolar membrane permeability will be of value in evaluating lysosome function in pathologic states." @default.
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- W2037741154 title "Membrane permeability of hepatic mitochondria and lysosomes studied by structure-linked enzyme changes" @default.
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- W2037741154 doi "https://doi.org/10.1016/0014-4800(73)90035-x" @default.
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