Hanna S, Kawamoto R, McNamee M, Baskin R J
Biochim Biophys Acta. 1981 Apr 22;643(1):41-54. doi: 10.1016/0005-2736(81)90217-0.
We have isolated sarcoplasmic reticulum from normal and dystrophic chicken muscle, using an improved isolation procedure. Dystrophic sarcoplasmic reticulum has a reduced level of calcium-sensitive ATPase activity, phosphoenzyme formation, and steady-state calcium transport. Anion-stimulated calcium transport by dystrophic sarcoplasmic reticulum is also reduced when measured under the proper conditions, and dystrophic sarcoplasmic reticulum shows no alteration in calcium efflux rate. Active calcium phosphate loading of the normal and dystrophic sarcoplasmic reticulum preparations indicates that a reduced percentage jof the dystrophic vesicles are capable of active calcium transport. The loaded dystrophic sarcoplasmic reticulum vesicles exhibit the same relative reductions in enzymatic activity as the starting sarcoplasmic reticulum preparations. However, the enzyme activities of normal and dystrophic sarcoplasmic reticulum are similar in the presence of detergent and exogenous phospholipid. On the basis of these results, we suggest that the lipid microenvironment of the dystrophic enzyme is altered.
我们采用改进的分离方法,从正常和营养不良的鸡肌肉中分离出肌浆网。营养不良的肌浆网中钙敏感ATP酶活性、磷酸酶形成和稳态钙转运水平降低。在适当条件下测量时,营养不良的肌浆网对阴离子刺激的钙转运也减少,且营养不良的肌浆网钙流出率无变化。正常和营养不良的肌浆网制剂的活性磷酸钙加载表明,营养不良的囊泡中能够进行活性钙转运的比例降低。加载后的营养不良肌浆网囊泡的酶活性相对降低程度与起始肌浆网制剂相同。然而,在存在去污剂和外源性磷脂的情况下,正常和营养不良肌浆网的酶活性相似。基于这些结果,我们认为营养不良酶的脂质微环境发生了改变。