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The effect of conditioning on the myofibrillar proteins of pork muscle
Author(s) -
Penny Ian F.
Publication year - 1976
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/jsfa.2740271211
Subject(s) - myofibril , tris , chemistry , conditioning , actin , troponin , biochemistry , biophysics , chromatography , biology , medicine , statistics , mathematics , myocardial infarction
Storage of pork muscle caused changes in the troponin complex of myofibrillar proteins. The changes were temperature dependent and progressive as conditioning proceeded. An alteration in actin also occurred but this became apparent only when myofibrils had been extracted with 5 m M Tris pH 8.2. About 60% of the proteins in an extract of myofibrils in 5 m M Tris pH 8.2 were bound to the precipitate formed with added F‐actin. After conditioning of the pork muscle, the amount of proteins in a Tris extract which were bound to added F‐actin was considerably reduced. Some of these changes were also observed in myofibrils which had been treated with a Ca 2+ activated proteinase.