Wikman-Coffelt J
Biochem J. 1980 Jan 1;185(1):265-8. doi: 10.1042/bj1850265.
The non-specific Ca2+-binding sites of skeletal-muscle myosin are located on the light chains; with the dissociation of light chains there is a corresponding decrease in the number of Ca2+-binding sites on light-chain-deficient myosin. The released light chains have a decreased binding affinity. Myosin heavy chains indirectly influence the Ca2+-binding properties of light chains by increasing the affinity of light chains for bivalent cations; this influence varies with pH. Because of light-chain dissociation at low Ca2+ and/or Mg2+ concentrations, anomalies may exist when analyses of non-specific Ca2+-binding properties of myosin are assessed by dialysis equilibrium.
骨骼肌肌球蛋白的非特异性钙离子结合位点位于轻链上;随着轻链的解离,缺乏轻链的肌球蛋白上的钙离子结合位点数量相应减少。释放的轻链具有降低的结合亲和力。肌球蛋白重链通过增加轻链对二价阳离子的亲和力间接影响轻链的钙离子结合特性;这种影响随pH值而变化。由于在低钙离子和/或镁离子浓度下轻链会解离,当通过透析平衡评估肌球蛋白的非特异性钙离子结合特性时,可能会出现异常情况。