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Change in Titin Position in Postmortem Bovine Muscle
Author(s) -
RINGKOB T. P.,
MARSH B. B.,
GREASER M. L.
Publication year - 1988
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.1365-2621.1988.tb10228.x
Subject(s) - titin , sarcomere , myofibril , anatomy , chemistry , nebulin , myosin , rigor mortis , biology , biophysics , myocyte , biochemistry , microbiology and biotechnology
Myofibrils were prepared from bovine psoas muscles removed from the carcass at 3 and 48 hr postmortem and subsequently stained with a monoclonal antibody against titin. The antibody stained 2 bands per sarcomere (perpendicular to the fiber direction) in myofibrils from 3‐hr muscle but often revealed 4 bands per sarcomere in the 48‐hr samples. The results suggested that (1) the titin shape might be altered within the first 2 days postmortem, or (2) proteolysis of titin or a protein to which it was attached occurred.