Decrease of 25 kD protein component in the muscle of myasthenia gravis
Objective To explore whether the protein components have difference between normal and myasthenia gravis (MG) skeletal muscles and the differential components of protein was associated with muscle contraction components. Methods Proteins were extracted from 10 cases of normal muscles and 17 cases of MG skeletal muscles with PBS and Gubstraub solution, respectively. The components of protein were analyzed by SDS-PAGE in common and micro methods in double blind. Composition of the differential protein band was discovered by two-dimensional electrophoresis. Results SDS-PAGE patterns showed that concentration of the protein band with mass of about 25 kD in the MG muscles were much lower than that in the normal muscles. The density of the protein band in the PBS extraction, in the common method, was 4.20±2.31 and 1.40±0.47 in the normal and MG muscles, respectively (p＜0.01), in the micro method, it was 4.62±1.94 and 1.66±0.56 in the normal and MG muscles. respectively (p＜0.001). The value of density for 25 kD protein band in the Gubstraub solution extraction, in the common analysis was 4.14 ± 1.33 and 2.02 ±1.08 in the normal and MG muscles, respectively (p＜0.001), and it in the micro analysis was 4.26±2.58 and l.34±0.79 in the normal and MG muscles, respectively (p＜0.001).The pattern of two-dimensional electrophoresis demonstrated that the differential 25 kD protein band consisted of two components at least with adjacent isoelectric point on the alkaline side in the gel, and they were proved to be irrelated to the components of myosin light chains. Conclusion It was suggested that 25 kD protein from skcletal muscle could be associated with the pathogeny or developing of MG.
skeletal muscles、differential protein、muscle contraction、myasthenia gravis、isoelectric point、double blind
8
R73;S7
2005-07-07（万方平台首次上网日期，不代表论文的发表时间）
共1页
87
