Okitani Akihiro, Ichinose Naoki, Koza Miki, Yamanaka Kensuke, Migita Koshiro, Matsuishi Masanori
Department of Food Science and Technology, Nippon Veterinary and Life Science University, Musashino-shi, Tokyo, Japan.
Biosci Biotechnol Biochem. 2008 Aug;72(8):2005-11. doi: 10.1271/bbb.80128. Epub 2008 Aug 7.
We investigated to determine why heating of squid muscle at 60 degrees C induced the liberation of actin from myofibrils. When a mixture of a myofibrillar fraction and a low-molecular sarcoplasmic fraction prepared from squid muscle was heated at 60 degrees C, actin liberation occurred. When a myofibrillar fraction was heated with ATP, AMP, or IMP, actin liberation occurred. Hence, AMP is perhaps one of the factors causing actin liberation in postmortem squid muscle. It was found that AMP and IMP reversibly dissociated actomyosin of chicken, bovine, and porcine skeletal muscles into actin and myosin on incubation at 0 degrees C at pH 7.2 in 0.2 M KCl. These results led us to conclude that AMP and IMP were the most responsible factors causing actin liberation from myofibrils in the heated muscle and causing reversible dissociation of actomyosin on storage of skeletal muscle at a low temperature. Hence, AMP and IMP are possible factors causing the resolution of rigor mortis in muscles.
我们进行了研究,以确定为何将鱿鱼肌肉在60摄氏度下加热会导致肌动蛋白从肌原纤维中释放出来。当将从鱿鱼肌肉制备的肌原纤维部分和低分子肌浆部分的混合物在60摄氏度下加热时,肌动蛋白会释放出来。当肌原纤维部分与ATP、AMP或IMP一起加热时,肌动蛋白也会释放出来。因此,AMP可能是导致死后鱿鱼肌肉中肌动蛋白释放的因素之一。研究发现,在0.2M KCl、pH 7.2、0摄氏度的条件下孵育时,AMP和IMP可使鸡、牛和猪的骨骼肌的肌动球蛋白可逆地解离为肌动蛋白和肌球蛋白。这些结果使我们得出结论,AMP和IMP是导致加热肌肉中肌动蛋白从肌原纤维释放以及骨骼肌在低温储存时肌动球蛋白可逆解离的最主要因素。因此,AMP和IMP可能是导致肌肉尸僵缓解的因素。