Mumps (MuV) and measles (MeV) virus cause mumps and measles in humans, both preventable by vaccination, but they are gaining importance in oncolytic virotherapy. Viral particle integrity and purity ensure efficacy and safety of such products, therefore their purification and concentration is exceptionally important both in biotechnology and basic research. The aims of this work are to investigate purification of MuV and MeV by hydrophobic interaction (HIC), ion-exchange (IEX) and immunoaffinity chromatography (IAC), ultracentrifugation (UC) and diafiltration (DF), investigate virus stability under used purification and storage conditions and investigate their lipidomes and proteomes. Results deem IEX unsuitable for MuV and MeV purification, while HIC and IAC yield relatively high recoveries of infective viruses (60-70%). Chromatographic yields are significantly influenced by initial virus sample heterogeneity. Analysis of virus proteomes confirmed the presence of all structural viral proteins and cellular proteins actin, annexins, cyclophilin A, integrin β1 and moesin, but their significance in virions remains to be determined.