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Conditioning of bovine muscle II.—Changes in the composition of extracts of myofibrils after conditioning
Author(s) -
Penny I. F.
Publication year - 1970
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.2740210608
Subject(s) - myofibril , conditioning , myosin , chemistry , tropomyosin , tris , actin , troponin , composition (language) , biochemistry , chromatography , medicine , statistics , linguistics , mathematics , philosophy , myocardial infarction
Myofibrils from longissimus dorsi muscles conditioned at 4° for 8 days and 15 days, were extracted by Hasselbach‐Schneider solution and 5 mM Tris‐HCl, pH 8·2. Both extractants removed increasing amounts of protein from the myofibrils as conditioning proceeded. More myosin, actin, tropomyosin and troponin was extracted by the Hasselbach‐Schneider solution and 5 mM Tris, pH 8·2, extracted increasing amounts of a complex mixture containing actin and α‐actinin. There was no evidence that any particular protein had been degraded or had disappeared and it is suggested that one of the effects of conditioning may have been an alteration in the binding of some of the proteins to each other in the myofibril.