The action of a muscle proteinase on the myofibrillar proteins of bovine muscle

The action of a muscle proteinase on the myofibrillar proteins of bovine muscle Myofibrillar proteins from bovine muscle have been treated with a Ca2+ activated muscle proteinase and the consequent changes in these proteins have been examined by various techniques. Tropomyosin, α‐actinin and troponin were substrates for the enzyme, the last losing its property of inhibiting actomyosin ATPase in the absence of Ca2+ ions. Actin and actomyosin were apparently not digested but the Mg2+‐activated ATPase activity of actomyosin was less after treatment whereas the Ca2+‐activated ATPase was unaffected. It is suggested that the observed destruction of the Z‐bands of the myofibrils by this proteinase is due to its digestion of the α‐actinin, rather than the actin component. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of the Science of Food and Agriculture Wiley

The action of a muscle proteinase on the myofibrillar proteins of bovine muscle

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Publisher
Wiley
Copyright
Copyright © 1974 John Wiley & Sons, Ltd
ISSN
0022-5142
eISSN
1097-0010
D.O.I.
10.1002/jsfa.2740251011
Publisher site
See Article on Publisher Site

Abstract

Myofibrillar proteins from bovine muscle have been treated with a Ca2+ activated muscle proteinase and the consequent changes in these proteins have been examined by various techniques. Tropomyosin, α‐actinin and troponin were substrates for the enzyme, the last losing its property of inhibiting actomyosin ATPase in the absence of Ca2+ ions. Actin and actomyosin were apparently not digested but the Mg2+‐activated ATPase activity of actomyosin was less after treatment whereas the Ca2+‐activated ATPase was unaffected. It is suggested that the observed destruction of the Z‐bands of the myofibrils by this proteinase is due to its digestion of the α‐actinin, rather than the actin component.

Journal

Journal of the Science of Food and AgricultureWiley

Published: Oct 1, 1974

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