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Conditioning of bovine muscle. III. The α‐actinin of bovine muscle
Author(s) -
Penny I. F.
Publication year - 1972
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.2740230317
Subject(s) - myofibril , conditioning , actinin , actin , chemistry , andrology , food science , anatomy , biology , biochemistry , medicine , cell , cytoskeleton , statistics , mathematics
The protein α‐actinin has been prepared, pure, from 1‐day‐old beef and from beef conditioned up to 21 days at +4 °C. The total amount of α‐actinin isolated frommyofibrils remained the same, 1.4% of the myofibril, regardless of the period of conditioning. A small reduction was found in the amount of α‐actinin, from conditioned muscle, which could be bound to F‐actin when compared with α‐actinin from fresh muscle, but the difference did not seem sufficient to explain all the changes in the properties of myofibrils occurring during conditioning.