1. Actin-binding peptide from smooth muscle myosin light chain kinase
- Author
-
Satoshi Kanoh, Masaaki Ito, Eiji Niwa, Yasushi Kawano, and Hartshorne, David J.
- Subjects
Actin -- Research ,Smooth muscle -- Analysis ,Myosin -- Analysis ,Proteolysis -- Observations ,Peptides -- Research ,Biological sciences ,Chemistry - Abstract
The smooth muscle myosin light chain kinase (MLCK) has an actin-binding site, which reveals a fall in the actin-binding capacity when the kinase at the N-terminal end of the molecule is hydrolyzed, as observed when thermolysin restricts proteolysis. A distinct actin-binding peptide is produced by different processes of cleavage. The actin-binding characteristics of the original MLCK are observed with the purification of the peptide. Resemblances to gizzard alpha-actinin and caldesmon are noted when contrasted with other actin-binding proteins.
- Published
- 1993