Article
Regulation of the erythrocyte Ca(2+)-ATPase by mutant calmodulins with Glu----Ala substitutions in the Ca(2+)-binding domains.
The Journal of biological chemistry - 5 Mar 1992
Bzdega T, Kosk-Kosicka D
Abstract excerpt
We have used four mutant calmodulins to study the regulation of human erythrocyte Ca(2+)-ATPase by the calmodulin-dependent pathway; the conserved Glu at position 12 in each of the four Ca(2+)-binding domains of calmodulin (Glu31, Glu67, Glu104, or Glu140) was replaced by Ala. At pCa 7, where unmodified calmodulin maximally activates the erythrocyte Ca(2+)-ATPase, all four mutants stimulated Ca(2+)-ATPase...
Topics
- Alanine
- Amino Acid Sequence
- Calcium
- Calcium-Transporting ATPases
- Calmodulin
- Cations, Divalent
- Enzyme Activation
- Erythrocytes
- Glutamine
- Humans
- Molecular Sequence Data