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Biochemical Properties of Actomyosin of Cold Stored Striated Adductor Muscles of Aulacomya ater ater (Molina)
Author(s) -
PAREDI MARÍA ELIDA,
MATTIO NORMA DE VIDO,
CRUPKIN MARCOS
Publication year - 1990
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.1365-2621.1990.tb03570.x
Subject(s) - myosin , chemistry , actin , myosin atpase , biophysics , striated muscles , myofibril , dissociation (chemistry) , food science , biochemistry , atpase , anatomy , biology , enzyme
Expressible juice showed highest increase within the second day of storage. Actomyosin was partially purified from stored muscles. Both reduced viscosity and Mg 2+ ‐ATPase activity of actomyosin decreased about 44% in the first day. These changes were due neither to actomyosin dissociation nor fragmentation of major proteins of the complex. Relative percentage of myosin decreased, and actin increased in actomyosin after the second day. These changes are related to a decrease in the myosin heavy chain and could explain the slow decrease in reduced viscosity and Mg 2+ ‐ATPase of this protein after the second day.