Effects of pH, ionic strength, and temperature on activation by calmodulin and catalytic activity of myosin light-chain kinase

Biochemistry ◽  
1982 ◽  
Vol 21 (10) ◽  
pp. 2386-2391 ◽  
Author(s):  
Donald K. Blumenthal ◽  
James T. Stull
Keyword(s):  
Catalytic Activity ◽  
Ionic Strength ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Effects Of Ph

scholarly journals Interaction between calmodulin and five different spin-labelled chlorophenothiazines

1986 ◽  
Vol 233 (3) ◽  
pp. 853-857 ◽  
Author(s):  
J L Olivier ◽  
D Rainteau ◽  
G Bereziat ◽  
C Wolf
Keyword(s):  
Ionic Strength ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Side Chain ◽  
Amino Group ◽  
Electrostatic Binding ◽  
Terminal Amino ◽  
Influence Of Ph ◽  
Derivatives Of

The binding to purified calmodulin of five spin-labelled derivatives of chlorophenothiazine was investigated by e.s.r. spectrometry and by the antagonizing potency on the calmodulin-dependent activation of myosin light chain kinase. The results of a comparative study and the influence of pH and ionic strength on the binding support the occurrence of an electrostatic binding involving the terminal amino group of the side-chain of the chlorophenothiazine. These results are discussed in relation to the specificity of the interaction that holds the antipsychotic drug-calmodulin complex together.

scholarly journals Purification and properties of myosin light-chain kinase from fast skeletal muscle

1977 ◽  
Vol 167 (1) ◽  
pp. 137-146 ◽  
Author(s):  
E M V Pires ◽  
S V Perry
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain Kinase ◽  
Myosin Light Chain ◽  
Similar Rate ◽  
Enzymic Activity ◽  
Fast Skeletal Muscle ◽  
Bivalent Cation ◽  
Purification And Properties ◽  
Effects Of Ph

1. A procedure is described for the isolation of myosin light-chain kinase from rabbit fast skeletal muscle as a homogeneous protein. 2. Myosin light-chain kinase is a monomeric enzyme of mol.wt. 77000. Under some conditions of storage it is converted into components of mol.wts. about 50000 and 30000 that possess enzymic activity. 3. The enzyme is clearly different in structure and properties from any other protein kinase so far isolated from muscle. 4. The enzyme is highly specific for the P-light chain (18000-20000-dalton light chain) of myosin and requires Ca2+ for activity. 5. The P-light chain is phosphorylated at a similar rate whether isolated or associated with the rest of the myosin molecule. 6. The effects of pH, bivalent cation and other nucleotides on the enzymic activity are described. 7. The role of the phosphorylation of the P-light chain of myosin in muscle function is discussed.

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