Vastus lateralis cytochrome oxidase activity and its relationship to maximal oxygen consumption in man

1974 ◽  
Vol 349 (4) ◽  
pp. 319-324 ◽  
Author(s):  
F. W. Booth ◽  
K. A. Narahara
Keyword(s):  
Oxygen Consumption ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Vastus Lateralis ◽  
Maximal Oxygen Consumption ◽  
Cytochrome Oxidase Activity

scholarly journals Effects of Chloramphenicol on the Mitochondrial Respiratory Chain in the Wild Strain and in a Cytoplasmic Chloramphenicol-Resistant Mutant ofTetrahymena pyriformis

1982 ◽  
Vol 2 (6) ◽  
pp. 715-719 ◽  
Author(s):  
Roland Perasso ◽  
Jean-Jacques Curgy ◽  
Nicole Stelly ◽  
Jean Andre
Keyword(s):  
Oxygen Consumption ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Wild Strain ◽  
Resistant Mutant ◽  
Wild Type ◽  
Mitochondrial Translation ◽  
Cytochrome Oxidase Activity ◽  
In The Wild ◽  
Mitochondrial Respiratory

The effects of chloramphenicol (CAP) on mitochondrial respiratory activity in the wild strain (ST) and in a cytoplasmic CAP-resistant mutant (STR1) ofTetrahymena pyriformiswere studied by determining oxygen consumption, by spectrophotometry, and by cytochemistry. In the absence of CAP both strains had the same respiration capacity, and the low-temperature spectra of their isolated mitochondria were similar. Furthermore, the mitochondria of both strains showed a positive reaction with diaminobenzidine, denoting a similar cytochrome oxidase activity. However, when cells were grown in CAP for 24 or 48 h, the peaks of cytochrome oxidase and cytochromebwere almost absent in the wild type. In this type the oxygen consumption was greatly decreased, and the mitochondria were no longer stained by diaminobenzidine. In the mutant, the peaks of cytochrome oxidase and cytochromebwere decreased only; respiration was less affected than in the wild type, and cytochrome oxidase activity was still disclosed by the diaminobenzidine reaction. These results show that CAP inhibits the synthesis of two cytochromes (band oxidase) which are partially translated into the mitochrondria ofT. pyriformis.In the mutant, CAP reduces only the mitochondrial translation, resulting in reduced mitochondrial activity and reduced growth rate of the cell. These results are compared with the nucleo-mitochondrial regulation mechanisms discussed in our previous works.

Correlation between blastocyst oxygen consumption and trophoblast cytochrome oxidase reaction at initiation of implantation of delayed mouse blastocysts

Development ◽  
1982 ◽  
Vol 71 (1) ◽  
pp. 75-82
Author(s):  
B. Ove Nilsson ◽  
Claes Magnusson ◽  
Sibylle Widéhn ◽  
Torbjörn Hillensjö
Keyword(s):  
Oxygen Consumption ◽  
Oxidative Phosphorylation ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Energy Production ◽  
Cytochrome Oxidase Activity ◽  
Uterine Secretion ◽  
Oxidase Reaction

Delayed blastocysts had an oxygen consumption of 0·24 nl/h, while only 4 h after an oestrogen injection the respiration had increased nearly two fold, remaining at this level both 8 and 18 h after activation for implantation. The mitochondria of delayed blastocysts exhibited no positive cytochrome oxidase reaction, neither in the trophoblast nor in the embryoblasts. A few mitochondria at 8 h and most of those of blastocysts activated for 18 h were positive. It is suggested that the activation of blastocysts for implantation is initiated by a surge of substrates for glycolysis into the uterine secretion causing an increased energy production by glycolysis which in turn makes possible an increase of the cytochrome oxidase activity of the mitochondria thus getting oxidative phosphorylation into action.

scholarly journals THE RESPIRATION AND CYTOCHROME OXIDASE ACTIVITY OF RAT AORTA IN EXPERIMENTAL HYPERTENSION

1959 ◽  
Vol 109 (2) ◽  
pp. 187-195 ◽  
Author(s):  
Marie M. Daly ◽  
E. Gambetta Gurpide
Keyword(s):  
Oxygen Consumption ◽  
Connective Tissue ◽  
Cytochrome Oxidase ◽  
Metabolic Activity ◽  
Oxidase Activity ◽  
Muscle Cells ◽  
Rat Aorta ◽  
Experimental Hypertension ◽  
Cytochrome Oxidase Activity

Oxygen consumption and cytochrome oxidase activity of aortas of rats with experimental hypertension were found to be higher than the corresponding values for aortas of normotensive animals. The higher metabolic activity of aortas of hypertensive animals appeared to be due both to an increase in the proportion of muscle cells to connective tissue fibers and to a higher activity of the intracellular portion of the tissue.

scholarly journals Effects of Chloramphenicol on the Mitochondrial Respiratory Chain in the Wild Strain and in a Cytoplasmic Chloramphenicol-Resistant Mutant of Tetrahymena pyriformis

1982 ◽  
Vol 2 (6) ◽  
pp. 715-719
Author(s):  
Roland Perasso ◽  
Jean-Jacques Curgy ◽  
Nicole Stelly ◽  
Jean Andre
Keyword(s):  
Oxygen Consumption ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Wild Strain ◽  
Resistant Mutant ◽  
Tetrahymena Pyriformis ◽  
Wild Type ◽  
Cytochrome Oxidase Activity ◽  
In The Wild ◽  
Mitochondrial Respiratory

The effects of chloramphenicol (CAP) on mitochondrial respiratory activity in the wild strain (ST) and in a cytoplasmic CAP-resistant mutant (STR 1 ) of Tetrahymena pyriformis were studied by determining oxygen consumption, by spectrophotometry, and by cytochemistry. In the absence of CAP both strains had the same respiration capacity, and the low-temperature spectra of their isolated mitochondria were similar. Furthermore, the mitochondria of both strains showed a positive reaction with diaminobenzidine, denoting a similar cytochrome oxidase activity. However, when cells were grown in CAP for 24 or 48 h, the peaks of cytochrome oxidase and cytochrome b were almost absent in the wild type. In this type the oxygen consumption was greatly decreased, and the mitochondria were no longer stained by diaminobenzidine. In the mutant, the peaks of cytochrome oxidase and cytochrome b were decreased only; respiration was less affected than in the wild type, and cytochrome oxidase activity was still disclosed by the diaminobenzidine reaction. These results show that CAP inhibits the synthesis of two cytochromes ( b and oxidase) which are partially translated into the mitochrondria of T. pyriformis. In the mutant, CAP reduces only the mitochondrial translation, resulting in reduced mitochondrial activity and reduced growth rate of the cell. These results are compared with the nucleo-mitochondrial regulation mechanisms discussed in our previous works.

Cytochrome Oxidase Activity at The Hepatic Parenchyma Different Periods of Ischemia and Obstructive Jaundice

2019 ◽  
Vol 9 (5) ◽  
pp. p8944
Author(s):  
Askarov Tahir Askarovich ◽  
Akhmedov Mirhalil Dzhalilovich ◽  
Fayziev Yokub Nishanovic ◽  
Ashurmetov Ahmadjon Makhamadjonovich ◽  
Dalimov Kenjabek Sabutaevich ◽  
...  
Keyword(s):  
Obstructive Jaundice ◽  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Hepatic Parenchyma ◽  
Cytochrome Oxidase Activity

Histochemical assessment of cytochrome oxidase activity for monitoring ischemic muscle injury

1985 ◽  
Vol 88 (2) ◽  
pp. 265-276 ◽  
Author(s):  
Richard M. Millis ◽  
Theodore A. Stephens ◽  
Gerard Harris ◽  
Columbus Anonye ◽  
Michael Reynolds
Keyword(s):  
Cytochrome Oxidase ◽  
Oxidase Activity ◽  
Muscle Injury ◽  
Cytochrome Oxidase Activity ◽  
Ischemic Muscle
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