Access the full text.
Sign up today, get DeepDyve free for 14 days.
N. Arakawa, D. Goll, J. Temple (1970)
MOLECULAR PROPERTIES OF POSTMORTEM MUSCLE. 8. Effect of Postmortem Storage on α‐Actinin and the Tropomyosin‐Troponin ComplexJournal of Food Science, 35
R. Da̧browska, B. Baryłko, E. Nowak, W. Drabikowski (1973)
The origin of 30,000 dalton protein in troponin preparationsFEBS Letters, 29
By Schaub, S. Perry (1969)
The relaxing protein system of striated muscle. Resolution of the troponin complex into inhibitory and calcium ion-sensitizing factors and their relationship to tropomyosin.The Biochemical journal, 115 5
R. Robson, D. Goll, N. Arakawa, M. Stromer (1970)
Purification and properties of α-actinin from rabbit skeletal muscle☆Biochimica et Biophysica Acta, 200
M. Stromer, D. Goll (1972)
Studies on purified -actinin. II. Electron microscopic studies on the competitive binding of -actinin and tropomyosin to Z-line extracted myofibrils.Journal of molecular biology, 67 3
I. Penny, C. Voyle, E. Dransfield (1974)
The tenderising effect of a muscle proteinase on beefJournal of the Science of Food and Agriculture, 25
C. Franzini-armstrong (1973)
THE STRUCTURE OF A SIMPLE Z LINEThe Journal of Cell Biology, 58
S. Perry, A. Corsi (1958)
Extraction of proteins other than myosin from the isolated rabbit myofibril.The Biochemical journal, 68 1
E. Hanson (1973)
Evidence from electron microscope studies on actin paracrystals concerning the origin of the cross-striation in the thin filaments of vertebrate skeletal muscleProceedings of the Royal Society of London. Series B. Biological Sciences, 183
R. Scopes, I. Penny (1971)
Subunit sizes of muscle proteins, as determined by sodium dodecyl sulphate gel electrophoresis.Biochimica et biophysica acta, 236 2
I. Penny (1970)
Conditioning of bovine muscle. II. Changes in the composition of extracts of myofibrils after conditioning.Journal of the science of food and agriculture, 21 6
C. Davey, K. Gilbert (1967)
Structural changes in meat during ageingInternational Journal of Food Science and Technology, 2
S. Ebashi, A. Kodama (1966)
Native tropomyosin-like action of troponin on trypsin-treated myosin B.Journal of biochemistry, 60 6
W. Busch, M. Stromer, D. Goll, Atsushi Suzuki (1972)
Ca2+-SPECIFIC REMOVAL OF Z LINES FROM RABBIT SKELETAL MUSCLEThe Journal of Cell Biology, 52
C. Davey, K. Gilbert (1968)
Studies in Meat Tenderness. 6. The Nature of Myofibrillar Proteins Extracted from Meat During AgingJournal of Food Science, 33
N. Arakawa, R. Robson, D. Goll (1970)
An improved method for the preparation of α-actinin from rabbit striated muscleBiochimica et Biophysica Acta, 200
R. Robson, D. Goll, M. Main (1967)
Molecular Properties of Post-Mortem Muscle.Journal of Food Science, 32
M. Greaser, J. Gergely (1973)
Purification and properties of the components from troponin.The Journal of biological chemistry, 248 6
F. Pepe (1966)
SOME ASPECTS OF THE STRUCTURAL ORGANIZATION OF THE MYOFIBRIL AS REVEALED BY ANTIBODY-STAINING METHODSThe Journal of Cell Biology, 28
J. Lecocq, G. Inesi (1966)
Determination of inorganic phosphate in the presence of adenosine triphosphate by the molybdo-vanadate method.Analytical biochemistry, 15 1
I. Penny (1972)
Conditioning of bovine muscle. 3. The -actinin of bovine muscle.Journal of the science of food and agriculture, 23 3
T. Masaki, M. Endo, S. Ebashi (1967)
Localization of 6S Component of α-Actinin at Z-bandJournal of Biochemistry, 62
C. Davey, M. Dickson (1970)
Studies in Meat Tenderness 8. Ultra-structural Changes in Meat During AgingJournal of Food Science, 35
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 of the Science of Food and Agriculture – Wiley
Published: Oct 1, 1974
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.