Abstract

Cd2 ion is known to uncouple mitochondrial oxidative phosphorylation and stimulate the ATPase at micromolar levels. The effect is reversed by 2,3-dimercaptopropanol but not by monothiols. We propose to label the cadmium binding component, probably a protein, with radioactive Cd2 ion, isolate it and characterize it. Its function will be determined after removal of the Cd2 ion by washing with excess 2,3-dimercaptopropanol. The implication of the Cd2 ion binding to its toxicity will be explored.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Environmental Health Sciences (NIEHS)
Type
Research Project (R01)
Project #
5R01ES002167-05
Application #
3249682
Study Section
Physical Biochemistry Study Section (PB)
Project Start
1980-01-01
Project End
1986-11-30
Budget Start
1984-12-01
Budget End
1986-11-30
Support Year
5
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
Boston Biomedical Research Institute
Department
Type
DUNS #
058893371
City
Watertown
State
MA
Country
United States
Zip Code

  Publications

Huang, Y; Kantham, L; Sanadi, D R (1987) Coupling factor B is a component of the Fo proton channel of mitochondrial H+-ATPase. J Biol Chem 262:3007-10
Huang, Y; Pringle, M J; Sanadi, D R (1985) Diamide blocks H+ conductance in mitochondrial H+-ATPase by oxidizing FB dithiol. FEBS Lett 192:83-7