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Effects of Postmortem Storage on Muscle Protein Degradation: Analysis by SDS‐Polyacrylamide Gel Electrophoresis
Author(s) -
KOOHMARAIE M.,
KENNICK W. H.,
ELGASIM E. A.,
ANGLEMIER A. F.
Publication year - 1984
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.1365-2621.1984.tb13732.x
Subject(s) - myofibril , tenderness , polyacrylamide gel electrophoresis , chemistry , electrophoresis , postmortem changes , gel electrophoresis , troponin t , polyacrylamide , troponin , biochemistry , food science , enzyme , medicine , pathology , myocardial infarction , polymer chemistry
Changes in myofibrillar proteins of bovine longissimus and semitendinosus muscles were examined during 14 days of postmortem storage at 2°C by SDS‐Polyacrylamide gel electrophoresis. Major changes in both muscles were: (1) appearance of a 95,000‐dalton component; (2) gradual disappearance of troponin‐T and gradual appearance of a 30,000‐dalton component; (3) gradual increase in intensity of a protein around 55,000‐daltons; and (4) gradual appearance of a 110,000‐dalton component. With the exception of the 95,000‐dalton component, the other changes have been reported previously by other authors. At the present time we have no knowledge of the origin of the 95,000‐dalton component, but it is known that calcium‐activated factor (CAF) is responsible for degradation of troponin‐T. Appearance of the 95,000‐dalton component during postmortem storage suggests involvement of CAF for increasing tenderness during postmortem storage.