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Spectrophotometry of b-type cytochromes in rat brain in vivo and in vitro

Spectrophotometry of b-type cytochromes in rat brain in vivo and in vitro 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 “hemoglobinfree” 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) http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

Spectrophotometry of b-type cytochromes in rat brain in vivo and in vitro

AJP - Cell Physiology , Volume 256: C840 – Apr 1, 1989

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Publisher
The American Physiological Society
Copyright
Copyright © 1989 the American Physiological Society
ISSN
0363-6143
eISSN
1522-1563
Publisher site
See Article on Publisher Site

Abstract

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 “hemoglobinfree” 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)

Journal

AJP - Cell PhysiologyThe American Physiological Society

Published: Apr 1, 1989

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