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Location of and post‐mortem changes in some cytoskeletal proteins in pork and cod muscle
Author(s) -
Morrison E Heather,
Bremner H Allan,
Purslow Peter P
Publication year - 2000
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/(sici)1097-0010(20000501)80:6<691::aid-jsfa590>3.0.co;2-t
Subject(s) - vinculin , nebulin , gadus , desmin , spectrin , actin , sarcolemma , cytoskeleton , myocyte , chemistry , biochemistry , anatomy , sarcomere , labelling , microbiology and biotechnology , biology , fish <actinopterygii> , titin , cell , immunohistochemistry , fishery , vimentin , immunology
The cytoskeletal proteins actin, nebulin, spectrin, desmin, vinculin and talin were labelled immunohistochemically in sections of muscle from commercially available pigs and cod ( Gadus morhua ) taken pre‐rigor and from samples stored for several days. Actin, nebulin and spectrin gave similar labelling patterns in both pork and cod muscle which remained the same in stored samples. Desmin was intensely labelled at the cell boundaries and within the body of the cells in both pork and cod in the initial and the stored samples. Vinculin was readily labelled in pork muscle but showed only diffuse labelling in fish. Labelling for talin in pork muscle was intense at the sarcolemma but was not present in samples stored for 4 days. In contrast, the label for talin was concentrated at the myotendinous junction of the cod muscle throughout the storage period. These are the first reports of the detection and location of spectrin and vinculin in fish muscle and of the location of talin. The results are discussed in terms of muscle structure, function and post‐mortem tenderisation. © 2000 Society of Chemical Industry