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J. Connell (1962)
Changes in amount of myosin extractable from cod flesh during storage at −14°Journal of the Science of Food and Agriculture, 13
Sayre Sayre, Briskey Briskey, Hoekstra Hoekstra (1963a)
Alteration of post‐mortem properties of porcine muscle by preslaughter heat treatment and diet modificationJ. Food Sci, 28
M. Urbin, Darrel Zessin, G. Wilson (1962)
Observations on a Method of Determining the Water Binding Properties of MeatJournal of Animal Science, 21
E. Briskey, R. Bray, W. Hoekstra, P. Phillips, R. Grummer (1960)
Effect of High Protein, High Fat and High Sucrose Rations on the Water-Binding and Associated Properties of Pork MuscleJournal of Animal Science, 19
Briskey Briskey, Sayre Sayre, Cassens Cassens (1962)
The development and application of an apparatus for continuous measurement of muscle extensibility and elasticity prior to and during the onset of rigor mortisJ. Food Sci, 27
Crepax Crepax (1951)
Sur le role de 1′ATP dans 1prime;extractablité des protéines musculairesBiochinz. et Biophys. Acta, 7
W. Partmann (1963)
Post‐Mortem Changes in Chilled and Frozen MuscleJournal of Food Science, 28
Grau Grau, Hamm Hamm (1953)
A simple method for the determination of water binding in musclesNaturwissenschaften, 40
J. Wismer‐Pedersen (1959)
QUALITY OF PORK IN RELATION TO RATE OF pH CHANGE POST MORTEMJournal of Food Science, 24
E. Briskey, J. Wismer‐Pedersen (1961)
Biochemistry of Pork Muscle Structure. 1. Rate of Anaerobic Glycolysis and Temperature Change versus the Apparent Structure of Muscle TissueJournal of Food Science, 26
R. Lawrie (1961)
Studies on the muscles of meat animals I. Differences in composition of beef longissimus dorsi muscles determined by age and anatomical locationThe Journal of Agricultural Science, 56
Wismer‐Pedersen Wismer‐Pedersen (1959)
Quality of pork in relation to rate of pH change post‐mortemFood Research, 24
J. Hill (1962)
Fibre Composition of Tough and Tender Muscles of Meat AnimalsNature, 196
E. Briskey, R. Sayre, R. Cassens (1962)
Development and Application of an Apparatus for Continuous Measurement of Muscle Extensibility and Elasticity Before and During Rigor Mortisa,a,bJournal of Food Science, 27
Hamm Hamm (1962)
The interaction between proteins and water and its importance for the colloid‐chemical qualities of meatFleischwirtschaft, 14
BY Dickerson, Medical Re (1960)
The effect of growth on the composition of avian muscle.The Biochemical journal, 75
R. Sayre, E. Briskey, W. Hoekstra (1963)
Effect of Excitement, Fasting, and Sucrose Feeding on Porcine Muscle Phosphorylase and Post‐Mortem GlycolysisJournal of Food Science, 28
E. Briskey, R. Bray, W. Hoekstra, P. Phillips, R. Grummer (1959)
The Effect of Exhaustive Exercise and High Sucrose Regimen on Certain Chemical and Physical Pork Ham Muscle CharacteristicsJournal of Animal Science, 18
E. Briskey, R. Sayre (1964)
Muscle Protein Extractability as Influenced by Conditions of Post-Mortem Glycolysis.∗Proceedings of the Society for Experimental Biology and Medicine, 115
J. Bendall, J. Wismer‐Pedersen (1962)
Some Properties of the Fibrillar Proteins of Normal and Watery Pork MuscleJournal of Food Science, 27
Hasselbach Hasselbach, Schneider Schneider (1951)
Der L‐myosin und Aktingehalt des KaninchenmuskelnBiochem. Z, 321
J. Dickerson, E. Widdowson (1960)
Chemical changes in skeletal muscle during development.The Biochemical journal, 74
A. Mirsky (1936)
THE CHANGE IN STATE OF THE PROTEINS OF MUSCLE IN RIGORThe Journal of General Physiology, 19
Helander Helander (1957)
On quantitative muscle protein determinationActa Physiol. Scand, 41
SUMMARY The solubilities of sarcoplasmic and myofibrillar proteins were determined at the time of slaughter, onset of rigor mortis, completion of rigor mortis and 24 hr after death in muscles exhibiting a wide range of physiological conditions during the post‐mortem period. Muscle protein solubility was grossly altered by the conditions of both temperature and pH which existed at the onset of rigor mortis or during the first few hours after death. Sarcoplasmic protein solubility at 24 hr was decreased to 55% of that found at 0 hr in muscle groups exhibiting high temperature and low pH at the onset of rigor mortis. Conversely, only a 17% reduction of sarcoplasmic protein solubility was noted in groups with high pH at onset. Myofibrillar protein solubility ranged from no reduction during the first 24 hr after death when pH remained high at onset to 75% reduction in muscle with low pH and high temperature at the onset of rigor mortis. The 24‐hr pH of the muscle appeared to have only a minor influence on protein solubility. Muscle protein solubility appeared to be one of the major factors affecting the juice‐retaining properties of muscle.
Journal of Food Science – Wiley
Published: Nov 1, 1963
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