Yamanoue M, Fei S, Okayama T
Department of Biofunctional Chemistry, Faculty of Agriculture, Kobe University, Japan.
Biosci Biotechnol Biochem. 1998 Apr;62(4):821-4. doi: 10.1271/bbb.62.821.
We found that paratropomyosin bound to beta-connectin, in examining binding of paratropomyosin at the junction of A- and I-bands of sarcomeres. The turbidity of a mixture of beta-connectin and paratropomyosin was greater with more paratropomyosin added, but high concentrations of Ca2+ suppress this increase. These results suggest that paratropomyosin is released from connectin filaments at the A-I junction region by increased concentrations of calcium ions in postmortem skeletal muscles.
在检查原肌球蛋白在肌节A带和I带交界处的结合情况时，我们发现原肌球蛋白与β-连接蛋白结合。随着添加的原肌球蛋白增多，β-连接蛋白和原肌球蛋白混合物的浊度增大，但高浓度的Ca2+会抑制这种增加。这些结果表明，在死后骨骼肌中，钙离子浓度升高会使原肌球蛋白在A-I交界区域从连接蛋白丝上释放出来。
