ＬＤＨ結合性免疫グロブリン３症例の生化学的検討

• 森山 隆則

  旭川医科大学附属病院検査部

• 細川 博道

  旭川医科大学附属病院検査部

• 信岡 学

  旭川医科大学附属病院検査部

書誌事項

タイトル別名

• The biochemical studies on the LDH linked immunoglobulin in three cases.

抄録

Biochemical properties of LDH linked immunoglobulin complexes found in sera of three cases (IgG-κ, IgA-κ, IgG-κ, λ) were studied. The complexes were completely dissociated by gel filtration at pH 3.0 and the dissociated LDH with normal molecular size showed a normal zymogram. When the dissociated immunoglobulins were incubated with each of the LDH isozymes (LDH_1-5), the two IgG type immunoglobulins recombined with all isozymes, but the IgA type immnoglobulin showed limited combination with only LDH_{2, 3, 4} fractions, indicating a difference in binding specificity between IgG and IgA.<br>Subclass specificity tested in two IgG types was not detected by Protein A affinity chromatography. The binding site of IgG was confirmed to exist on the Fab portion by the method of papain digestion. 5'-AMP-Sepharose 4 B affinity chromatography revealed different affinity between LDH linked IgG (broad pattern) and LDH linked IgA (extra band). This finding suggests the presence of conformational heterogeneity.

収録刊行物

• 生物物理化学

  生物物理化学 29 (3), 197-203, 1985

  日本電気泳動学会

キーワード

• LDH anomaly
• LDH linked immunoglobulin
• dissociation
• recombination
• 5'-AMP-Sepharose 4 B

詳細情報

• CRID: 1390001204203523584
• NII論文ID: 130003606701
• NII論文ID: 80002451769
• DOI: 10.2198/sbk.29.197
• ISSN: 13499785
• ISSN: 00319082
• Web Site: https://search.jamas.or.jp/link/ui/1986000134
• 本文言語コード: ja
• データソース種別:
  • JaLC
  • Crossref
  • CiNii Articles
• 抄録ライセンスフラグ: 使用不可