Separation Of Myosin Heavy Chain Isoforms Research Articles

Method for Enhanced Separation of Cardiac Myosin Heavy Chain Isoforms by Nongradient SDS-PAGE

Current methods of SDS-PAGE for cardiac myosin heavy-chain (MHC) isoforms are complex and require more than 24 h. The aim of the current study was to improve the methodology of gel electrophoresis for faster and efficient separation of MHC isoforms. Rat ventricle and soleus tissues were subjected to sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) using tris-glycine buffer. Matrix-assisted laser desorption ionization (MALDI)–time of flight (TOF)–mass spectra (MS) of protein bands was done to identify α,β-MHC. Clear separation of α,β-MHC isoforms on SDS-PAGE was achieved and identity was confirmed by MALDI-TOF-MS. The smaller gel system drastically reduced the total run time to 2 h. The present method provides a simple, quick, and efficient protocol for cardiac α,β-MHC separation.

Analysis of skeletal and cardiac muscle from desmin knock‐out and normal mice by high resolution separation of myosin heavy‐chain isoforms

In this study, using a modified electrophoretic technique, we have defined in the mouse the myosin heavy-chain composition of both newborn and adult skeletal and cardiac muscles. Using this high resolution technique it was possible to detect modifications in the myosin heavy-chain expression in both cardiac and skeletal muscles of desmin knock-out mice.

Analysis of skeletal and cardiac muscle from desmin knock-out and normal mice by high resolution separation of myosin heavy-chain isoforms

In this study, using a modified electrophoretic technique, we have defined in the mouse the myosin heavy-chain composition of both newborn and adult skeletal and cardiac muscles. Using this high resolution technique it was possible to detect modifications in the myosin heavy-chain expression in both cardiac and skeletal muscles of desmin knock-out mice.