Article
Site-directed mutagenesis of glutamine residue of calmodulin. Activation of guanylate cyclase of Tetrahymena plasma membrane.
The Journal of biological chemistry - 15 Apr 1990
Nagao S, Matsuki S, Kanoh H, Ozawa T, Yamada K, Nozawa Y
Abstract excerpt
Tetrahymena calmodulin (CaM) differs from mammalian CaM in its ability to activate Tetrahymena guanylate cyclase. Of 12 differences in amino acid sequence, two occur near the carboxyl terminus (Gln-143----Arg and Thr-146----deletion). To investigate the functional significance of the carboxyl-terminal region in activation of the guanylate cyclase, three mutated CaMs were engineered by using cassette mutagenesis...
Topics
- 3',5'-Cyclic-AMP Phosphodiesterases
- Amino Acid Sequence
- Animals
- Base Sequence
- Brain
- Calmodulin
- Cell Membrane
- DNA, Recombinant
- Enzyme Activation
- Genetic Techniques
- Glutamine