2024-03-28T11:41:11Z
https://niigata-u.repo.nii.ac.jp/oai
oai:niigata-u.repo.nii.ac.jp:00024122
2022-12-15T03:54:17Z
453:456
471:537:538:1233
Characterization of the surface antigens on human mononuclear cells to which anti-myelin associated glycoprotein (MAG) monoclonal antibodies bind
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
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
荒井, 元美
144532
monoclonal antibody
myelin-associated glycoprotein
mononuclear cells
surface marker
モノクローナル抗体
ミエリン糖蛋白
リンパ球
表面抗原
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.
departmental bulletin paper
新潟医学会
1987-06
application/pdf
新潟医学会雑誌
6
101
382
389
新潟医学会雑誌
AN00182415
00290440
https://niigata-u.repo.nii.ac.jp/record/24122/files/101(6)_382-389.pdf
jpn