A new light chain for myosin-7
نویسندگان
چکیده
منابع مشابه
Myosin light-chain phosphatase.
1. A method for the isolation of a new enzyme, myosin light-chain phosphatase, from rabbit white skeletal muscle by using a Sepharose-phosphorylated myosin light-chain affinity column is described. 2. The enzyme migrated as a single component on electrophoresis in sodium dodecyl sulphate/polyacrylamide gel at pH7.0, with apparent mol.wt. 70000. 3. The enzyme was highly specific for the phosphor...
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Myosin light-chain kinase (MLCK) of smooth muscle is multifunctional, being composed of N-terminal actin-binding domain, central kinase domain, and C-terminal myosin-binding domain. The kinase domain is the best characterized; this domain activates the interaction of smooth-muscle myosin with actin by phosphorylating the myosin light chain. We have recently shown that the Met-1-Pro-41 sequence ...
متن کاملStructural requirement of the regulatory light chain of smooth muscle myosin as a substrate for myosin light chain kinase.
The substrate structure required for skeletal and smooth muscle myosin light chain kinases (MLC kinase) was studied by using various mutant regulatory light chains of smooth muscle myosin. The deletion of the NH2-terminal 10 residues did not greatly affect the kinetic parameters of smooth MLC kinase; however, deletion of an additional 3 residues, Lys11-Arg13, prevented phosphorylation. In contr...
متن کاملEffects of relaxin on rat uterine myosin light chain kinase activity and myosin light chain phosphorylation.
Isometrically suspended uteri from estrogen-primed rats were stimulated with prostaglandin F2 alpha and then exposed to relaxin. Relaxin-dependent decreases in the ratio of phosphorylated to total myosin light chains (MLC) and in MLC kinase activity, measured in the presence of 0.5 mg/ml of uterine myosin and the absence and presence of Ca2+-calmodulin (CaM), were observed. The time-course and ...
متن کاملMyosin light chain kinase and myosin light chain phosphatase from Dictyostelium: effects of reversible phosphorylation on myosin structure and function
We have partially purified myosin light chain kinase (MLCK) and myosin light chain phosphatase (MLCP) from Dictyostelium discoideum. MLCK was purified 4,700-fold with a yield of approximately 1 mg from 350 g of cells. The enzyme is very acidic as suggested by its tight binding to DEAE. Dictyostelium MLCK has an apparent native molecular mass on HPLC G3000SW of approximately 30,000 D. Mg2+ is re...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2020
ISSN: 0021-9258
DOI: 10.1074/jbc.h120.014595