FOOD SCIENCE ›› 2004, Vol. 25 ›› Issue (12): 50-54.

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Extraction and Purification of Myosin from Rabbit Skeletal Muscles and Its Solution Turbidity and Solublility

 HAN  Min-Yi, XU  Xing-Lian, LIN  Li-Jun, ZHOU  Guang-Hong   

  1. Key Laboratory of Agricultural and Animal Products Processing and Quality Control,Ministry of Agriculture,Nanjing Agriculture University
  • Online:2005-12-15 Published:2011-10-24

Abstract: The myosin was extracted and purified from Pasoas major (PM) and Semimembranosus proprius (SMp) of male rabbit, and effects of myosin concentration, pH, ionic strength, and heating temperature on the turbidity and solubility of PM and SMp myosin were studied. The results showed that concentration of the purified myosin was about 20~30mg/ml, the rate of extraction was about 1%. Four bands were observed in the purified myosin SDS-PAGE pattern, which were assigned to one myosin heavy chains (MHC) and three myosin light chains,with molecular weight of 205, 25.9, 17.8 and 13.8kDa, respectively. The results showed that the effect of myosin concentration on turbidity was linear. The turbidity reached its maximum at pH5. 5 and in 0.6mol/L KCl. The solubility increased significantly when pH value was greater than pH5.0. The turbidity increased and the solubility decreased with the decrease of the ionic strength. The turbidity increased with the increase of temperature under the same myosin concentration. PM and SMp myosin turbidity reached the maximum at 55℃ and 60℃ respectively. The solubility decreased when the temperature increased.

Key words: myosin, rabbit, extraction, purification, turbidity, solubility, Pasoas major, Semimembranosus propriu, rabbit skeletal muscle