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Role of Light Chains In Heat‐Induced Gelation of Skeletal Muscle Myosin
Author(s) -
MORITA JUNICHIRO,
OGATA TOMOHIRO
Publication year - 1991
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1991.tb05398.x
Subject(s) - myosin , actin , immunoglobulin light chain , myosin light chain kinase , skeletal muscle , chemistry , biophysics , ionic strength , myosin head , biochemistry , anatomy , biology , organic chemistry , immunology , antibody , aqueous solution
ABSTRACT More than 60% of alkali light chains were released from rabbit skeletal myosin during heating to form gel. The removal of about 1 mol of regulatory light chain (LC2)/mol of myosin (LC2‐deficient myosin) resulted in major decrease of gel strength at low ionic strength. The F‐actin concentration required to attain maximum gel strength of the LC2‐deficient myosin was greater than that of control myosin. These changes in functional characteristics of myosin induced by removal of LC2 were restored by reassociation of LC2 to the LC2‐deficient myosin. Results showed skeletal myosin LC2 has an important role in its heat‐induced gelation.