Monitoring Myosin Degradation During Conditioning in Chicken Meat Using an Immunological Method |
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Authors: | Y Ikeuchi K Kamiyama A Suzuki T Hirose K Kim T Hayashi T Ito |
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Affiliation: | Authors Ikeuchi, Hayashi, and Ito are affiliated with the Lab. of Chemistry and Technology of Animal Products, Dept. of Bioscience and Biotechnology, Graduate School of Agriculture, Kyushu University, Fukuoka, 812-8581, Japan.;Authors Kamiyama, Suzuki, Hirose, and Kim are with the Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University, Niigata, 950-2181, Japan. |
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Abstract: | ABSTRACT: Changes of chicken breast myosin during storage at 2°C and 37°C were monitored immunochemically. Anti-myosin subfragment-1 (S-1) monoclonal antibody, which recognized epitopes within the 27 kDa fragment of S-1, and the anti-myosin rod polyclonal antiserum, were prepared. Myosin degradation products were not detected in muscle extracts stored for 3 weeks at 2°C. In contrast, storage at 37°C brought about the degradation of myosin heavy chain to immunologically detectable small fragments. While, myosin rod produced during the conditioning period was not decomposed into any small filaments. Namely, storage of muscle at 37°C resulted in minor amounts of myosin heavy chain degradation, with initial conversion to rod and S-1 fragments, and subsequent breakdown occurred in the S-1 region only. Immunoblot assay also suggested that the pattern of changes in myosin heavy chain in muscle incubated at 37°C was similar to that produced by in vitro digestion with cathepsin D. |
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Keywords: | chicken muscle conditioning immunoblot myosin degradation cathepsin |
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