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altering the normal anatomic and functional STUDIES biological oxidations in vivo depend on accurate identification intracellular compounds that produce absorption changes during electron transport reactions. Most intracellular hemoproteins, in their reduced forms, have specific absorption bands that can be used to monitor oxidation-reduction (redox) reactions under appropriate experimental conditions. The absorpOPTICAL tion characteristics the intramitochondrial cyto- chromes have been studied extensively in mammalian tissues for more than 50 years (15). Most optical studies s, however, are conducted with isolated tissues, cells, or subcellular organelles because spectral changes by hemoglobin or other pigments, as well as nonspecific light scattering, interfere with changes in absorption specific to intracellular redox events in living tissues (24). Advances in optical technology over the years have provided new insights into the behavior s in situ (4, 14). In addition to advancements made with improved optical methods, hemoglobin artifacts can be minimized now by replacing the blood with oxygencarrying perfluorochemical compounds that maintain tissue viability and permit study intracellular events C840 0363-6143/89 $1.50 characteristics the tissue (10, 22). In âhemoglobinfreeâ rats, inhibitors the terminal enzyme complex (-c oxidase) the mitochondrial respiratory chain produced very different redox responsesin cerebral cortex. Cerebral redox responses to cyanide (CN)
AJP - Cell Physiology – The American Physiological Society
Published: Apr 1, 1989
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