Access the full text.
Sign up today, get DeepDyve free for 14 days.
T. Yasui, T. Fukazawa, Koui Takahashi, M. Sakanishi, Y. Hashimoto (1964)
Phosphate Effects on Meat, Specific Interaction of Inorganic Polyphosphates with Myosin BJournal of Agricultural and Food Chemistry, 12
O. Lowry, N. Rosebrough, A. Farr, R. Randall (1951)
Protein measurement with the Folin phenol reagent.The Journal of biological chemistry, 193 1
M. Schaub, D. Hartshorne, S. Perry (1967)
The adeonosine-triphosphatase activity of desensitized actomyosin.The Biochemical journal, 104 1
M. Fujimaki, N. Arakawa, A. Okitani, O. Takagi (1965)
The Changes of “Myosin B” (“Actomyosin”) During Storage of Rabbit Muscle. II. The Dissociation of “Myosin B” into Myosin A and Actin, and its Interaction with ATPJournal of Food Science, 30
C. Wu (1969)
Comparative studies on myosins from breast and leg muscles of chicken.Biochemistry, 8 1
B. Ames, D. Dubin (1960)
The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid.The Journal of biological chemistry, 235
J. Hay, R. Currie, F. Wolfe (1972)
THE EFFECT OF AGING ON PHYSICOCHEMICAL PROPERTIES OF ACTOMYOSIN FROM CHICKEN BREAST AND LEG MUSCLEJournal of Food Science, 37
I. Penny (1974)
The action of a muscle proteinase on the myofibrillar proteins of bovine muscle.Journal of the science of food and agriculture, 25 10
J. Hay, R. Currie, F. Wolfe (1973)
POLYACRYLAMIDE DISC GEL ELECTROPHORESIS OF FRESH AND AGED CHICKEN MUSCLE PROTEINS IN SODIUM DODECYLSULFATEJournal of Food Science, 38
A. Weber (1956)
The ultracentrifugal separation of L-myosin and actin in an actomyosin sol under the influence of ATP.Biochimica et biophysica acta, 19 2
Weber Weber (1956)
The ultracentrifugal separation of l‐myosin and actin in an actomyosin sol under the influence of ATPBiochem. Biophys. Acta., 19
Gebald Offer, Cabl Moos, R. Starr (1973)
A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization.Journal of molecular biology, 74 4
J. Jones (1972)
Studies on chicken actomyosin. I. Effect of storage on muscle enzymic and physico-chemical properties.Journal of the science of food and agriculture, 23 8
Offer Offer, Moos Moos, Starr Starr (1973)
A new protein of the thick filaments of vertebrate skeletal myofibrilsJ. Mol. Biol., 74
Haga Haga, Maruyama Maruyama, Noda Noda (1965)
Formation of actomyosin during the extraction of muscle mince with Weber‐Edsall solutionBiochem. Biophys. Acta., 94
K. Weber, M. Osborn (1969)
The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis.The Journal of biological chemistry, 244 16
Sarah Hitchcock, Hugh Huxley, A. Szent-Györgyi (1973)
Calcium sensitive binding of troponin to actin-tropomyosin: a two-site model for troponin action.Journal of molecular biology, 80 4
Yamamoto Yamamoto, Hosokawa Hosokawa, Samejima Samejima (1974)
Effect of freezing on the myofibril from hen breast musclesJ. Coll. Dairying, 5
ABSTRACT The ATP dissociation of natural actomyosin from chicken breast and leg muscle at 0 and 168 hr postmortem was studied by ultracentrifugal and viscometric methods. Superprecipitation behavior and ATPase activities were also examined. The results demonstrate that postmortem aging of muscle has no effect on the dissociation of actin and myosin, and are incompatible with the hypothesis that the actin‐myosin interaction undergoes a “weakening” during postmortem aging.
Journal of Food Science – Wiley
Published: Mar 1, 1976
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.