Open AccessCalcium‐Sensitivity of Pig‐Carotid‐Actomyosin ATPase in Relation to Phosphorylation of the Regulatory Light Chain
Author(s) -
MRWA Ulrike,
TROSCHKA Monika,
GROSS Christiane,
KATZINSKI Lothar
Publication year - 1980
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1980.tb04328.x
Subject(s) - phosphorylation , myosin light chain kinase , immunoglobulin light chain , myosin , chemistry , atpase , papain , biochemistry , calcium , biophysics , actin , microbiology and biotechnology , biology , enzyme , organic chemistry , antibody , immunology
Ca 2+ ‐dependent phosphorylation of the 20000‐ M r regulatory light chain was found to be a necessary condition for the Ca 2+ ‐sensitivity of the Mg 2+ ‐dependent ATPase activity and super‐precipitation of pig carotid actomyosin. Actin‐myosin interaction independent of phosphorylation and Ca 2+ (ATPase activity and superprecipitation) were demonstrated in aged actomyosin preparations and in preparations from which the regulatory light chains were removed by papain digestion.