@article{oai:niigata-u.repo.nii.ac.jp:00024122,
 author = {荒井, 元美},
 issue = {6},
 journal = {新潟医学会雑誌, 新潟医学会雑誌},
 month = {Jun},
 note = {Three (GC-J4, MC-P2 and MC-P4) out of five murine monoclonal antibodies (mAbs) to myelin-associated glycoprotein (MAG) bound to human mononuclear cells (MNC). The results of the competitive inhibition assay suggested that MC-P2 and MC-P4 bind directly to or close to the Leu 7 epitope, and that GC-J4 binds to the epitope which is distinct from the Leu 7 epitope. The electrophoretic patterns of immunoprecipitates with GC-J4, MC-P2 and anti-Leu 7 from detergent lysates of surface labeled human MNC were very similar. The target molecules of anti-Leu 7, MC-P2 and GC-J4 have apparent molecular weights of 205, 170, 150, 135, 110, 85, 65 and 55 kDa, and they are monomeric or noncovalently associated proteins. The patterns of immunoprecipitates with MC-P4 were slightly different from those with anti-Leu 7 and MC-P2. The implications of these results are as follows: 1) The mAb with specificity to the carbohydrate part of MAG reacts with the Leu 7-reactive molecule on human MNC. 2) At least two epitopes detected by anti-MAG mAbs coexist on the surface molecules with various apparent molecular weights. 3) The fine antigenic specificity of MC-P4 is different from those of anti-Leu 7 or MC-P2.},
 pages = {382--389},
 title = {抗Myelin-associated glycoprotein(MAG)モノクローナル抗体と結合するヒトのリンパ球表面抗原の解析},
 volume = {101},
 year = {1987}
}