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Comparative studies on the biochemical characteristics of natural actomyosin isolated from PSE and normal pork

Yu-ting Ding1, Wei-guo Sang, Yan Chen

  • 1College of Biology & Environment Engineering, Zhejiang University of Technology, Hangzhou 310014, China. dingyt@mail.hz.zj.cn

Journal of Zhejiang University. Science
|April 22, 2004
PubMed

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Actin is a highly conserved cytoskeletal protein found abundantly in eukaryotic cells. It constitutes 10% weight of the total cellular protein in muscle cells, while in non-muscle cells, it is lower and makes up around 1–5 percent of the total cell protein. Actin found in the unicellular amoebae and complex multicellular animals is around 80% similar, demonstrating their conservation over a billion years of evolution.  Actin coding genes are conserved within species and across different species.
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Myosins are a family of molecular motor proteins, first identified in the skeletal muscles, where they are responsible for muscle contraction. Along with their role in muscle contraction, these proteins also play a role in the intracellular transport of molecules and vesicles. There are twenty-four classes of myosins based on their domain sequence and organization. Of the twenty-four, six classes (Myosin I, Myosin II, Myosin V, Myosin VI, Myosin VII, and Myosin X)  have been well characterized.