IMMUNOGLOBULINS OF DOG : Identification of Seven Immunoglobulins and Sequence of their Antibody Response
スポンサーリンク
概要
- 論文の詳細を見る
Independent from the recent publication of Johnson and Vaughan (1967), investigations had been made about canine antibodies. Seven immunoglobulins each possessing antigenically distinct heavy chain and common light chain were identified and their structure and sequence of antibody responses were examined. Hyperimmunized dog serum with bovine serum albumin (BSA) demonstrated at least seven different radioactive bands with I^<131>-labelled antigen in radioimmunoelectrophoresis. All of these precipitin bands also reacted with I^<131>-labelled anti-dog L chain. Partial purification of each immunoglobulin was performed by the combination of sodium sulfate precipitation, DEAE-cellulose column chromatography and gel-filtration on Sephadex G200 or Sepharose 4B column. Antigenic structure and antibody activities were examined by immunodiffusion and radioimmunoelectrophoresis techniques. In immunoelectrophoresis and radioimmunoelectrophoresis three cross-reactive precipitin bands (γG_1, γG_2 and γG_3) with antibody activity appeared in γ_2 region. All three showed cross-reactivity with human γG globulin and were considered to be subclasses of dog γG globulin. Purified γG globulin had sedimentation coefficient (S_<20, W>) of 6.7S in analytical ultracentrifugation. In papain digestion and 2-mercaptoethanol treatment, dog γG globulin showed comparable chain structure with human or rabbit γG globulin. Four precipitin bands each possessing antibody activity were found in γ_1 region each having distinct H chain and common L chain. One of them with 17.6S (S_<20, W>) and cross-reactive with human γM globulin equalled to γM globulin of dog. Among other three γ1 globulins, major immunoglobulin showed sdimentation coefficient of 6.6S and was designated γ_<la> globulin. This protein showed no cross-reactivity with human γG, γA, γM and D-myeloma protein and was considered to be a unique immunoglobulin in dog. The other two minor γ1 globulins (γ_1b, γ_1c) were eluted a little faster from Sephadex G200 column than γG or γ_1a and considered to have slightly larger molecular size. The sequence of antibody response to BSA in these seven immunoglobulins was examined by radioimmunoelectrophoresis. The antibody activity was first appeared in γG_1 and γG_2 precipitin bands, next in γG_3 and γ_la. The activity of γG class decreased whereas that of γ_1a increased according to prolongation of immunization and became a major antibody in the hyperimmune period. Antibody activity of hyperimmunized dog serum with BSA was mainly in γ_la globulin and this antiserum did not show distinct precipitin reaction and passive hemagglutination. Nevertheless it had been proved this antiserum had the activities to inhibit the precipitin reaction and passive hemagglutination of rabbit antibody to BSA at high dilution.
- 日本アレルギー学会の論文
- 1969-01-30
著者
関連論文
- 227. 培養癌細胞に対するリンパ球の細胞障害作用に関する研究(老化・腫瘍・遺伝)
- 3. 流血中腫瘍細胞と胸管内リンパ液細胞(II 一般講演(流血,髄液中の異型細胞), 第6回 日本臨床細胞学会講演要旨)
- 229. 腫瘍特異免疫の in vitro 誘導と 2-mercaptoethanol の影響(老化・腫瘍・遺伝)
- 226. immunoblastic lymphadenopathy と考えられた5症例(老化・腫瘍・遺伝)
- IMMUNOGLOBULINS OF DOG : Identification of Seven Immunoglobulins and Sequence of their Antibody Response