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MMP13 (Collagenase 3) is a member of the matrix metalloproteinase (MMP) family. In pathology it is overexpressed in rheumatoid arthritis (RA), osteoarthritis (OA) and human carcinomas. It is secreted in its inactive proforms from which it can be activated. The project studies how MMP13 can degrade/digest the normal femoral head human articular cartilage. Peptides were separated using reversed phase chromatography coupled on-line with various mass spectrometry techniques including ion trap, quadropole Time-Of-Flight (Q-TOF) and triple quadropole (QQQ) instruments. Guanidine hydrochloride (GuHCl) was used to extract proteins from the cartilage tissue. Sodium dodecyl sulfate poly acrylamide gel electrophoresis was used also to give visualize similarities and differences between the control and the MMP13 treated sample. MMP13 showed an effect on both media (released proteins from the cartilage tissue via the buffer solution) and a little effect on the cartilage tissue (pellet). The main result showed that the tissue sample preparation was critical in order to obtain sufficient release of proteins. The powderisation of tissue was much better in releasing proteins than intact tissue plugs probably due to larger contact area and shorter diffusion distance