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J. Bendall (1951)
The shortening of rabbit muscles during rigor mortis: its relation to the breakdown of adenosine triphosphate and creatine phosphate and to muscular contractionThe Journal of Physiology, 114
H. Levy, N. Sharon, E. Ryan, D. Koshland (1962)
Effect of temperature on the rate of hydrolysis of adenosine triphosphate and inosine triphosphate by myosin with and without modifiers. Evidence for a change in protein conformation.Biochimica et biophysica acta, 56
R. Locker (1960)
DEGREE OF MUSCULAR CONTRACTION AS A FACTOR IN TENDERNESS OF BEEFJournal of Food Science, 25
R. Davies, D. Cain, A. Delluva (1959)
THE ENERGY SUPPLY FOR MUSCLE CONTRACTION *Annals of the New York Academy of Sciences, 81
B. Marsh (1954)
Rigor mortis in beefJournal of the Science of Food and Agriculture, 5
E. Lundsgaard (1950)
The ATP content of resting and active muscleProceedings of the Royal Society of London. Series B - Biological Sciences, 137
D. Fremery, M. Pool (1960)
BIOCHEMISTRY OF CHICKEN MUSCLE AS RELATED TO RIGOR MORTIS AND TENDERIZATIONJournal of Food Science, 25
Isolated fresh beef muscles have been found to shorten more at 2° than at 37°. Minimum shortening occurs in the temperature region of 14–19°. At higher temperatures shortening coincides with the onset of rigor mortis but at low temperatures it begins rapidly and usually immediately. This shortening is reversible. Three different beef muscles show this effect but two rabbit muscles do not.
Journal of the Science of Food and Agriculture – Wiley
Published: Nov 1, 1963
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