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POSTMORTEM CHANGES IN CYTOSKELETAL ELEMENTS OF FISH MUSCLE 1
Author(s) -
BUSCONI LILIANA,
FOLCO EDUARDO J.,
MARTONE CELINA B.,
SANCHEZ JORGE J.
Publication year - 1989
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1989.tb00411.x
Subject(s) - myofibril , cytoskeleton , nebulin , ultrastructure , anatomy , chemistry , fish <actinopterygii> , electron microscope , skeletal muscle , actin , biophysics , sarcomere , myocyte , biology , microbiology and biotechnology , biochemistry , titin , cell , fishery , physics , optics
Transmission electron microscopic examination of samples from fresh and 7 days‐cold‐stored white croaker skeletal muscle did not reveal apparent changes in overall structure of contractile elements of muscle. However, when purified myofibrils obtained from fresh and stored muscles were extracted with 0.6 M KI and the residues were examined in the scanning electron microscope, a progressive disappearance of exosarcomeric longitudinal filaments connecting successive Z structures was observed. Electrophoretic analysis of myofibrillar proteins obtained from fresh and stored muscles showed a marked degradation of nebulin, a major component of the endosarcomeric cytoskeletal network, whereas the other protein constituents of myofibrils remained practically unchanged. These alterations in elements of both cytoskeletal lattices of muscle may have important effects on physical properties of fish meat.