scholarly journals Inter-Relationships between Proton Electrochemical Gradient, Adenine-Nucleotide Phosphorylation Potential and Respiration, during Substrate-Level and Oxidative Phosphorylation by Mitochondria from Brown Adipose Tissue of Cold-Adapted Guinea-Pigs

1977 ◽  
Vol 75 (2) ◽  
pp. 601-612 ◽  
Author(s):  
David G. NICHOLLS ◽  
Vibeke S. M. BERNSON
2019 ◽  
pp. 331-343
Author(s):  
Jean Himms-Hagen ◽  
Nicole Bégin-Heick ◽  
Anna-Lisa Kates ◽  
Joan Triandafillou ◽  
Masoud Ghorbani ◽  
...  

1973 ◽  
Vol 51 (10) ◽  
pp. 751-758 ◽  
Author(s):  
H. M. C. Heick ◽  
C. Vachon ◽  
Mary Ann Kallai ◽  
Nicole Bégin-Heick ◽  
J. LeBlanc

Groups of animals were treated with injections of isopropylnoradrenaline, thyroxine, or both hormones together. The effects of these hormonal treatments on the size, protein content, and level of some mitochondrial enzymes, in particular the cytochrome oxidase, were determined and compared to the effect on these parameters produced by cold adaptation. The changes observed were correlated with the resistance of the animals to cold stress and with their metabolic response to injections of isopropylnoradrenaline. All treatments increased the size of the brown adipose tissue. Whereas thyroxine had little effect on the protein content and cytochrome oxidase, both isopropylnoradrenaline and cold adaptation produced increases in these parameters. It appears that the isopropylnoradrenaline-treated animals mimic more closely the cold-adapted animals than do those with thyroxine treatment. However, the isopropylnoradrenaline-treated animals are not as resistant to cold as the cold-adapted animals.


1970 ◽  
Vol 118 (1) ◽  
pp. 171-179 ◽  
Author(s):  
W. N. Aldridge ◽  
B. W. Street

1. The binding of trimethyltin and triethyltin to rat liver mitochondria was determined and the results were analysed by the method of Scatchard (1949). 2. One binding site (site 1) has the correct characteristics for the site to which trimethyltin and triethyltin are attached when they inhibit oxidative phosphorylation. For each compound the concentration of site 1 is 0.8nmol/mg of protein and the ratios of their affinity constants are the same as the ratio of the concentrations inhibiting oxidative phosphorylation. 3. Binding site 1 is present in a fraction derived from mitochondria containing only 15% of the original protein. In this preparation ultrasonication rapidly destroyed site 1. 4. Dimethyltin and diethyltin do not prevent binding of triethyltin to rat liver mitochondria, whereas triethyl-lead does. 5. Trimethyltin and triethyltin bind to mitochondria from brown adipose tissue and the results indicate a binding site 1 similar to that in rat liver mitochondria. 6. The advantages and limitations of this approach to the study of inhibitors are discussed.


2014 ◽  
Vol 42 (3) ◽  
pp. 259-269 ◽  
Author(s):  
Emine Ercikan Abali ◽  
Sangita Phadtare ◽  
Jim Galt ◽  
Barbara Brodsky

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