Phosphorylation of myosin light chain by protease activated kinase I |
| |
Authors: | Polygena T Tuazon James T Stull Jolinda A Traugh |
| |
Institution: | 1. Department of Biochemistry University of California Riverside, California 92521 USA;2. Department of Pharmacology University of Texas Health Science Center Dallas, Texas 75235 USA;3. Moss Heart Center University of Texas Health Science Center Dallas, Texas 75235 USA |
| |
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. |
| |
Keywords: | |
本文献已被 ScienceDirect 等数据库收录! |