Post translational modifications due to HG. Myofilament (pellet) and non-myofilament (supernatant) proteins were separated by centrifugation of tissue homogenate. A. Lysine acetylation was not detected for any myofibrillar protein except two unidentified proteins at <20 kDa. These were not differentially acetylated between HG and nonHG. B. Advanced glycation end-products (AGEs), detected by Western blots of anti-pentosidine probe, demonstrated similarly low AGEs accumulation in myofilament fraction between HG and nonHG. AGEs accumulation of non-myofilament proteins appeared in two proteins at ~27 kDa and ~55 kDa, but was highly variable and not different between HG and nonHG.