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Differential binding of rabbit fast muscle myosin light chain isoenzymes to regulated actin
Author(s) -
Trayer Hylary R.,
Trayer Ian P.
Publication year - 1985
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(85)81065-6
Subject(s) - myosin , ionic strength , actin , biophysics , myosin light chain kinase , differential centrifugation , chemistry , actina , ionic bonding , isozyme , binding site , biochemistry , biology , ion , cytoskeleton , enzyme , organic chemistry , aqueous solution , cell
The direct binding of S1(A1) and S1(A2) to regulated actin has been investigated by centrifugation. Binding was measured in the presence of either Mg·Ado PP [NH] P or Mg·ADP at 24°C at various ionic strengths. At low ionic strength, in either the presence or absence of Ca 2+ , the binding of S1(A1) to regulated actin was always stronger than for S1(A2). As the ionic strength was increased the differential binding between S1(A1) and S1(A2) was still maintained in the presence of Ca 2+ but not in its absence. These data are discussed in terms of a modifying role for the N‐terminal region of the A1 light chain in regulation of the contractile process.