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The binding of skeletal muscle C‐protein to regulated actin
Author(s) -
Yamamoto Katsuhiro
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81545-9
Subject(s) - actin , protein filament , myofibril , actin binding protein , biophysics , chemistry , actin remodeling , skeletal muscle , microbiology and biotechnology , actin cytoskeleton , cytoskeleton , biochemistry , biology , anatomy , cell
The binding of C‐protein, a component of thick filament of myofibrils, to regulated actin filaments in the presence or absence of CA 2+ was studied. The amount of C‐protein bound to regulated actin filaments in the presence of CA 2+ was higher than those in the absence of Ca 2+ . The addition of C‐protein to regulated actin caused an increase in turbidity, especially in the presence of Ca 2+ , and this was found to result from side‐by‐side association of actin filaments into bundles. In the absence of Ca 2+ , no actin filament bundles were formed.