Abstract
Protease activated kinase I from rabbit reticulocytes has been shown to phosphorylate the P-light chain of myosin light chains isolated from rabbit skeletal muscle. The enzyme is not activated by Ca2+ and calmodulin or phospholipids. Protease activated kinase I is not inhibited by trifluoperazine at concentrations up to 200 μM or by the antibody to the Ca2+, calmodulin-dependent myosin light chain kinase from rabbit skeletal muscle. Two-dimensional peptide mapping of chymotryptic digests of myosin P-light chain show the site phosphorylated by the protease activated kinase is different from that phosphorylated by the Ca2+, calmodulin-dependent myosin light chain kinase.
Original language | English (US) |
---|---|
Pages (from-to) | 910-917 |
Number of pages | 8 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 108 |
Issue number | 2 |
DOIs | |
State | Published - Sep 30 1982 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology