Pyridine nucleotide oxidases and transhydrogenase in acclimatization to high altitude
- 1 February 1961
- journal article
- research article
- Published by American Physiological Society in American Journal of Physiology-Legacy Content
- Vol. 200 (2) , 351-354
- https://doi.org/10.1152/ajplegacy.1961.200.2.351
Abstract
Activities of pyridine nucleotide oxidases and transhydrogenase have been examined in heart, liver and rectus femoris muscle of guinea pigs native to sea level and high altitude. There was found an enhanced reduced form of diphosphopyridine nucleotide oxidase (DPNH-oxidase) and transhydrogenase activity in heart and muscle from animals adapted to high altitude. In muscle the higher activity at altitude was due solely to increase in ratio of red to white portions. Both groups showed the pigmented portion twice as active as the white one. In liver, neither the DPNH-oxidase system nor the transhydrogenase were significantly changed in their activities on a fresh weight basis. Nevertheless, the DPNH-oxidase is higher at altitude when the activity is expressed per gram of nitrogen. The reduced form of triphosphopyridine nucleotide oxidase activity was not appreciably changed in any of the studied tissues. It was concluded that adaptation to high altitude is associated with apparent changes in the magnitude of the electron transport pathway. Increased activity in skeletal muscle is probably related to the tissue pigment content.Keywords
This publication has 4 references indexed in Scilit:
- Tissue Pigment Manifestations of Adaptation to High AltitudesAmerican Journal of Physiology-Legacy Content, 1957
- PHOSPHORYLATIVE AND NONPHOSPHORYLATIVE PATHWAYS OF ELECTRON TRANSFER IN RAT LIVER MITOCHONDRIAProceedings of the National Academy of Sciences, 1956
- The relation of energy-rich phosphate in muscle to myoglobin and to cytochrome-oxidase activityBiochemical Journal, 1953
- The activity of the cytochrome system in muscle and its relation to myoglobinBiochemical Journal, 1953