IRRADIATION OF MEAT PROTEIN.
Technical rept. (Final), 1 Jun 66-31 Dec 67,
AGRICULTURAL RESEARCH COUNCIL LANGFORD (UNITED KINGDOM) MEAT RESEARCH INST
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The classical method for extraction and purification of myosin was modified so as to protect the enzyme from oxidation and to prevent actomyosin formation. Using this method, salt solutions of myosin from the sterno mandibularis muscle of the beef animal were prepared. Irradiation of these solutions resulted in rapid aggregation of the protein adenosine triphosphatase activity increased at doses below 100 Krad while above this level the enzyme was destroyed, the 50 inactivation dose being about 250 Krad. Polyamino acids were used as model compounds in experiments to investigate 1 the effects of radical scavengers on amino acid destruction and amide formation, 2 the exchange of tritium from tritiated water, and 3 interactions with hydrated electrons and hydroxyl radicals. The results of these experiments showed that hydroxyl radicals are responsible for the major part of the destruction. The mechanism of the reactions leading to destruction, the effects of oxygen and the possibility of a repair mechanism involving back-reactions between polyamino acid radicals and hydrated electrons are discussed. In addition, effects of temperature on certain reactions were studied. Author
- Food, Food Service and Nutrition
- Radiation and Nuclear Chemistry