@article{oai:niigata-u.repo.nii.ac.jp:00006672, author = {Tanaka, Masami and Tanaka, Keiko and Nishizawa, Masatoyo and Inuzuka, Takashi and Baba, Hiroko and Sato, Shuzo and Miyatake, Tadashi}, issue = {2}, journal = {Acta medica et biologica, Acta medica et biologica}, month = {Sep}, note = {We examined the reactivity of five murine monoclonal antibodies against myelin-associated glycoprotein (MAG) with the measles virus. One of the three antibodies recognizing the carbohydrate moiety of MAG and human mononuclear cells (MC-P2) could react with the measles ELISA antigen but another two reacting with peptide moiety could not. Eleven murine monoclonal antibodies against human lymphocytes including anti-Leu-7, and anti-MAG monoclonal IgM from a patient with demyelinating polyneuropathy could not react with the measles ELISA antigen. However, in an immunoblotting study, two bands, 56 kDa and 63 kDa, were stained by MC-P2, which differed from those -H(78 kDa), P(69 kDa) and NP(60 kDa) - stained by the serum of a patient with subacute sclerosing panencephalitis. It may be possible that the antigens reacting with MC-P2 are derived from Vero cells used in a culture of measles virus. Anti-MAG monoclonal murine antibody (MC-P2) could NOT react with measles virus proteins. Although previously we have found in studying by inhibition assay, that MC-P2 bind directly to or close to the Leu-7 epitope, a chemical feature of the antigen of MC-P2 and Leu-7 seems to be different.}, pages = {53--61}, title = {The characterization of murine monoclonal antibodies against myelin-associated glycoprotein (MAG) of the human brain : II The difference of the antigenic determinant between clone, MC-P2, reacting with human natural killer cells and Leu-7}, volume = {35}, year = {1987} }