Sarcopenia is the rapid loss of muscle mass and strength during ageing. It can have a severe effect on the quality of life of the elderly. Exercise can protect and to a certain degree replace some of the lost muscle mass, but at a certain point the muscles’ population of stem cells are depleted and muscle can no longer be rebuilt. Several factors are thought to cause sarcopenia such as reduced hormone levels, altered protein metabolism, degeneration of the nervous system and lifestyle. Some other diseases that can cause muscle wasting such as Duchenne muscular dystrophy and type-II diabetes are known to have altered protein glycoslylation. With all this in mind we are studying the changes in the aged muscle glycoproteome. To do this a combination of 2-D gel electrophoresis and blotting were used to separate and immobilise proteins to a nitrocellulose membrane while peroxide-conjugated lectins were used to identify particular types of carbohydrate moieties on the muscle proteins. N-linked glycoslylation can play many vital roles in the way a protein functions; it can affect protein folding, protein degradation, targeting of proteins to intracellular organelles, as well as more widespread functions such as cell-cell communication. So through this work we are hoping to identify changes in the glycoslylation and understand its effects on muscle ageing.