@article{mbs:/content/journal/jgv/10.1099/0022-1317-69-8-2061, author = "Gerlier, Denis and Garnier, Florence and Forquet, Frederique", title = "Haemagglutinin of Measles Virus: Purification and Storage with Preservation of Biological and Immunological Properties", journal= "Journal of General Virology", year = "1988", volume = "69", number = "8", pages = "2061-2069", doi = "https://doi.org/10.1099/0022-1317-69-8-2061", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-69-8-2061", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "purification", keywords = "haemagglutinin", keywords = "measles virus", abstract = "Summary Measles virus envelope haemagglutinin (H) was purified rapidly with Triton X-100-solubilized virions by a two-step anion-exchange chromatography using fast protein liquid chromatography. The purity of the glycoprotein in its dimeric form was demonstrated by SDS-PAGE followed by silver staining or autoradiography. The purified H glycoprotein was further freed from contaminating detergent by dialysis of octylglucoside detergent. This purification procedure, together with subsequent lyophilization and storage at -70°C of the H glycoprotein which was incorporated into phospholipid vesicles allowed the full preservation of its haemagglutinating activity, its reactivity with a monoclonal anti-H antibody that recognized a conformational epitope and its capacity to elicit anti-H antibodies with haemagglutination-inhibiting and neutralizing activities.", }