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JPH0348699A - 二特異性およびオリゴ特異性の一価およびオリゴ価リセプター、それらの調整および使用 - Google Patents

二特異性およびオリゴ特異性の一価およびオリゴ価リセプター、それらの調整および使用

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Publication number
JPH0348699A
JPH0348699A JP2165485A JP16548590A JPH0348699A JP H0348699 A JPH0348699 A JP H0348699A JP 2165485 A JP2165485 A JP 2165485A JP 16548590 A JP16548590 A JP 16548590A JP H0348699 A JPH0348699 A JP H0348699A
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JP2978210B2 (ja
Inventor
Klaus Dr Bosslet
クラウス、ボスレット
Peter Hermentin
ペーター、ヘルメンツィン
Gerhard Seemann
ゲルハルト、ジーマン
Ludwig Kuhlmann
ルートウィッヒ、クールマン
Axel Steinstraesser
アレックス、シュタインシュトレーサー
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Siemens Healthcare Diagnostics GmbH Germany
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Behringwerke AG
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    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
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Abstract

(57)【要約】本公報は電子出願前の出願データであるた
め要約のデータは記録されません。

Description

【発明の詳細な説明】 〈発明の分野〉 本発明は、過当なリンカ−によって、二つまたはそれ以
上の異なる特異性の抗体のＦ　（ａｂ）断片をコードす
るＤＮＡの融合による遺伝子操作によって調製される、
二特異性（ｂｉｓｐｅｃｉｆｉｃ）およびオリゴ特異性
（ｏｌｉ８ｏｓｐｅｃｉｆｉｃ）の−価（ｍｏｎｏｖａ
　ｌ　ｅｎｔ）およびオリゴ価（ｏｆ　ｉｇｏｖａｌｅ
ｎｔ）リセブターに間する。これに関して、一つの特異
性は、好ましくは、細胞膜上または間隙に位置している
種度関連抗原（ＴＡＡ）のエピトープに向けられるかま
たは腫瘍内皮（ＴＥ）のエピトープに向けられるが、そ
の他の特異性は高分子量または低分子量のリガンド（Ｉ
　ｉｇａｎｄ）に関連して、例えば、キレートのエチレ
ンジアミン四酢酸塩（ｅｔｈｙｌｅｎｅｄｉａｍｉｎｅ
ｔｅｔｒａ−ａｃｅｔａｔｅ）およびジエチレントリア
ミン五酢酸塩（ｄｉｅｔｈｙｌｅｎｅｔｒｉａｍｉｎｅ
ｐｅｎｔａ−ａｃｅｔａｔｅ）のＹ９０複合型（各々、
ＥＤＴＡ−Ｙ２ＯおよびＤＴＰＡ−Ｙ２Ｏ）と反応する
。特に好ましい態様においては、キレートとの結合は、
ｆｏｓ−ｊｕｎ相互作用（または他にはアビデイン−ビ
オチン（ａｖｉｄｉｎ−ｂｉｏｔｉｎ）相互作用）を介
して、キレートリセブターの腕部（ａｒｍ）上で起きる
。他の好ましい特異性は、触媒的な性質を有する、ある
いは同じ腫瘍細胞上の他のＴＡＡとまたはリンパ球細胞
上のリセプターと結合する。
〈従来の技術〉 二特異性抗体は、今日まで、次の方法で調製されてきた
。
異種三機能性（ｈｅｔｅｒｏｂｉｆｕｎｃｔｉｏｎａｌ
）リンカ−を介する多種（ｄｉｖｅｒｓｅ）特異性の抗
体の化学的結合　（）１．　Ｐａｕｌｕｓ：　Ｂｅｈｒ
ｉｎｇｎｓｔ、Ｍｉｔｔ、７８．１１８−１３２．１９
．８５）既に人手可能で、種々のモノクローナル抗体（
ＭＡ　ｂ　）を分泌するバイブリドの融合、および二特
異性の一価の部分の単離（Ｕ、Ｓ。
５ｔａｅｒｚおよび門、Ｊ、　Ｂｅｖａｎ：　Ｐｒｏｃ
、　Ｎａｔ１、　Ａｃａｄ、　Ｓｃｉ、　ＵＳＡ　８３
．１４５３−１４５７．１９８６）二つの異なるＭＡｂ
の重鎖および軽鎖遺伝子（４個の遺伝子）のネズミミエ
ローマ細胞または他の真核細胞発現系へのトランスフェ
クション、および二特異性−価部分の単離（ｕ、　Ｚｉ
ｍｍｅｒｍａｎｎ：　Ｒｅｖ、　Ｐｈｙｓｉｏ、　Ｂｉ
ｏｃｈｅｍ。
Ｐｈａｒｍａｃｏ１、　１０５．１７６−２６０．１９
８Ｇ、　Ｊ、　ｖａｎＤｉｊｋら：ｌｎｔ、　Ｊ、　Ｃ
ａｎｃｅｒ　４３．３４４−３４９．１９８９）この型
の二特異性抗体は、悪性腫瘍の治療および診断に用いら
れる。方法の原理は、第一′段階において、長期にわた
って大量投与量で二特異性巨大分子（ｍａｃｒｏｍｏｌ
ｅｃｕｌｅ）を注射することによって、標的細胞上で二
つの特異性の中の一つによって認識されるエピトープの
飽和を達成することからなる。
数日間の治療の中断からなる第二段階において、非特異
的に吸着した二特異性抗体の非標的Ｍｉ織からの自己除
去（ａｕｔｏｅｌ　１ｍ１ｎａｔｉｏｎ）がある。この
自己除去は、糖残基、好ましくはガラクト−ス、に結合
している抗イデイオタイプ抗体の注射によって加速する
ことができ、二特異性リセプターの抗ｌ！瘍腕部に対し
て向けられる。
方法の第三段階は放射性同位元素で標識した親水性低分
子量リガンドの静脈内注射からなるが、このリガンドは
、細胞内で蓄積せず、体内停留時間が短く、９１１Ｙ、
　ｌｌ１６Ｒｅ、ＩｆｌｌｌＲｅ、＋８９Ｒｅ１９９Ｉ
ＩＴｃまたは口Ｉ　１　ｎなどのβ−“およびγ−エミ
ッターの複合定数（ｃｏｍｐｌｅｘｉｎｇ　ｃｏｎｓｔ
ａｎｔ）が高く、かつ二特異性すセブタ一の第二の特異
性に高い親和性で結合する。この段階の結果、標的組織
上での保持が延長されるとともに放射性リガンドの濃縮
が行われ、その結果、標的組織の選択的崩壊がなされて
、例えば、転移（ｍｅｔａｓｔａｓｅｓ）の診断が可能
になる。
Ｈ、＝８ 本発明は、要求に応じて、特定のエピトープとの一価ま
たはオリゴ価結合部位を有しており、過当なリンカ−に
よる遺伝子操作によって産生される、二特異性およびオ
リゴ特異性リセブターを今提供する。
すなわち、抗体ａおよびｂのＶ□およびＣＨ１部分をコ
ードする遺伝子断片を、例中の表１に示されるような過
当な合成オリゴヌクレオチドを用いて、ＭＡｂｂのＶ８
ドメイン（ｄｏｍａｉｎ）のＮ末端をポリペプチドスペ
ーサーを介してＭＡｂａのＣＨ１ドメインのＣ末端に共
有結合で結合させるようにして、連結させる（第１図）
。ｖ１４ａＣＨ１ａ−ポリペプチドスペーサー−ＶＨｂ
ＣＨｌ　ｂ遺伝子構築物を、抗体ａおよびｂの軽鎖の遺
伝子とともに真核細胞（例えばマウスミエローマ細胞）
にトランスフェクト（ｔｒａｎｓｆｅｃｔ）させるｏ　
Ｃ）Ｉｌ　ａ、　Ｃ，１ｂ、　Ｃ，ａおよびＣ，ｂドメ
インを、反対荷電が定常ドメイン（Ｃ＋１　ａ　（＋　
）　Ｃｘａ　（）、ＣＨｌｂ（−）ＣＫｂ　（＋））（
＋、：陽性、−＝陰性）と接触領域で合わさるように、
または、接触の反対領域が各場合に疎水性または各場合
に親水性であるようにして、修飾する。これは、トラン
スフェクトされたもの（形質転換体、ｔｒａｎｓｆｅｃ
ｔｏｍａｓ）が、重鎮および軽鎖の正しい対合を有する
バイブリド分子を選択的に発現することを意味する（第
２図）。
ここで、抗体ａは抗腫瘍抗体の代表的な例で、抗体すは
低分子量りガント、好ましくはキレートＤＴＰＡ−Ｙ９
０またはＥＤＴＡ−Ｙ２Ｏ、に対する抗体を表すもので
ある。
従って、二特異性またはオリゴ特異性リセブターは、過
当なリンカ−を介しての、多種特異性の抗体のｖ８およ
びＣＨｌドメインの遺伝子工学的な構築を意味し、これ
によれば、対応する軽鎖との結合のための要求される移
動性（ｍｏｂｉｌｉｔｙ）が存在して、抗原結合が妨げ
られない。
抗原結合部位は、　結合価（ｖａｎｌｅｎｃｉｅｓ）ま
たは結合部位と呼ばれる。二特異性−価リセプターは、
したがって、二つの特異性がある場合には各場合に一つ
の抗原結合部位を有する。したがって、二特異性三価リ
セプターは、一つの特異性のための一つの抗原結合部位
を、他の特異性のために二つの抗原結合部位を各々有す
る。
腫瘍抗原（ＭＡｂａ）に対して二価であ２てＥＤＴＡ−
Ｙ２Ｏ（ＭＡｂ　　ｂ）に対して一価である二特異性リ
セプターを、上記のオリゴヌクレオチドリンカーを用い
て、上記の重鎮遺伝子構築物をＭＡｂａの■８およびＣ
，１ドメインをコードする遺伝子部分に連結させること
によって調製して（第３図）、ポリペプチドスペーサー
によ７てＭＡｂ　　ｂのＣＨｌドメインのＣ末端をＭＡ
ｂａのｖＨドメインのＮ−末端に連結するようにする。
これらの遺伝子構渠物を、ＭＡｂａおよびｂに属する軽
鎖の遺伝子とともに真核細胞（例えばミエローマ細胞）
にトランスフェクトさせる。上記のようにして、Ｃ，４
１およびＣ，ドメインは、相補的な荷電または各場合に
疎水性または親水性である接触領域とともに提供される
。形質転換体は、ＭＡｂａの二つのＦ　（ａｂ）断片お
よびＭＡｂ　　ｂの一つのＦ　（ａｂ）断片（第４図）
を含む融合分子を選択的に発現する。ペプチドリンカ−
の移動性は、ＭＡｂａの二つのＦ　（ａｂ）腕部の腫瘍
細胞に対する整列（ａｉｉｇｎｍｅｎｔ）、同時に、細
胞間空間に対するＭＡｂ　　ｂのＦ　（ａｂ）腕部の整
列を可能にする。同様に、同一または異なる特異性のさ
らなる結合部位を加えることが可能である。さらに、構
築物中の特異性の配列（５ｅｑｕｅｎｃｅ）を自由に組
み合わせることが可能である。
したがって、本発明は、例えばＴＡＡまたはＴＥのよう
な、細胞膜上または間隙中に位置するエピトープのため
の特異性と、細胞外空間にのみ分布する低分子量または
高分子量リガンドのための特異性とを共に有する、二特
異性またはオリゴ特異性、−価またはオリゴリセブター
に間する。これに関連して、一つの特異性は、独国特許
出願第９３９０９７９９．４号明細書において提示され
たように、好ましくは腫瘍特異性抗体によって形成され
、他の特異性は、好ましくは、ＤＴＰＡ−Ｙ２Ｏまたは
Ｅ　Ｄ　Ｔ　Ａ−Ｙ　９０に対して向けられる。特に好
ましい態様においては、結合はキレートと、ｆｏｓ−ｊ
ｕｎ相互作用（例５を参照されたい）を介してキレート
リセブター腕部上で起きる。他の好ましい本発明の変形
は、触媒的活性を有する特異性の組み入れからなる。さ
らに、二つの特異性を有する三価の第４図の例で示され
るように、特異性の配列または結合価の選択に制限はな
い。
本発明の特に好ましい構築物は、表２．３．４および／
または５の■遺伝子を含むものである。
これらの配列有する抗体およびそれらの性質は、独国特
許出願第ｐ　３９０９７９９．４号明細書に記載されて
いる。さらに、相補性決定領域（ＣＤＲ）は、Ｋａｂａ
ｔおよびＷｕ　（Ｓｅｑｕｅｎｃｅｓ　ｏｆ　Ｐｒｏｔ
ｅｉｎｓ　ｏｆＩｍｍｕｎｏｌｏｇｉｃａｌ　Ｉｎｔｅ
ｒｅｓｔ、　ＵＳ　Ｄｅｐｔ、　ｏｆ　）Ｉｅａｌｔｈ
ａｎｄ　Ｈｕｍａｎ　５ｅｒｖｉｃｅｓ、　ＵＳ　Ｇｏ
ｖｅｒｎｍｅｎｔ　ＰｒｉｎｔｉｎｇＯｆｆｉｃｅ、１
９８７）の方法によって同定することができる。同様に
好ましい構築物は、上記のモノクローナル抗体によフて
定義されたエピトープに対する特異性を含むものである
。
加えて、本発明は、上記の構築物の調製のための遺伝子
工学的方法、および標的細胞の抑制および診断のための
医薬物の調製のための上記構築物の使用に間する。すな
わち、第一の段階において、構築物を注射した後に標的
細胞上で関連エピトープを飽和させて、次いで、非特異
的に吸着したあるいは非結合の構築物を除去する。これ
に続く次の段階は、注射および次いでの低または高分子
量リガンドの特異的結合からなるが、このリガンドは、
細胞内に蓄積されず、本質的に細胞毒性（ｃｙｔｏｔｏ
ｘｉｃ）または適宜に他の段階において身体外（ｅｘｔ
ｒａｃｏｒｐｏｒｅａｌ）の影響によッテ細胞毒性に「
活性化」されるものである。この型の方法の例は、酵業
的活性化、プロドラッグのマイクロ波照射による活性化
またはレーザー光線による活性化などがある。
本発明は、ざらに語例および特許請求の範囲に示される
通りである。
例」」−抗−ＤＴＰＡ−Ｙ２ＯまたはＥＤＴＡ−Ｙ９０
ＭＡｂの調製 イソチオシアネートベンジル−ＤＴＰＡ（化学式２式％ 法によってヒト血清アルブミン（ＨＳＡ、キャリアとし
て）に、Ｈ９Ａ分子当り１９個のベンジル−ＤＴＰＡの
誘導化（ｄｅｒｉｖａｔｉｚａｔｉｏｎ）率で、ハブテ
ンとして共有結合させた。冷却したＹを中に複合させて
おいたこのハブテン−キャリア複合体の２０μｇを、０
日目にフロイントのアジュバントとともに、７日および
１４日目に不完全フロインドアジュバントとともに、お
よび２１日目にＰＢＳとともに、Ｂａ１ｂ／ｃマウスに
皮下注射した。
２４日目に、最高値の抗−ＤＴＰＡ抗体タイターを示す
マウスの牌臓を、ＳＰ２１０−Ａｇ１４ミエローマ細胞
系（Ｓｈｕｌｍａｎら：　Ｎａｔｕｒｅ　２７６．２６
９．１９７８）と融合させた。得られるバイプリドーマ
を、ＤＴＰＡおよびＥＤＴＡに対する高親和性のＭＡｂ
の産生についてＤＴＰＡ−特異性ＥＬＩＳＡ中で試験し
た。ＥＬＩＳＡは、ＨＳＡ−ベンジル−ＤＴＰＡ−Ｙを
含む溶液を負荷した固相からなる。
試験されるＭＡｂを含む上清を遊離のキレートまたはそ
の金属イオン複合体と予備インキュベートしてから、特
異的固相との結合を測定した。抗−マウス免疫グロブリ
ン抗体と結合している酵素増幅系を、この目的のために
用いた。これらの方法の詳細は付録１ａおよび１ｂに記
載の通りである。
付録１ｅに記載の性質を有するＭＡｂは、この分析系を
用いて得られた。
他の多くの抗−ＤＴＰＡ／ＥＤＴＡ　ＭＡｂと対照的に
、これらＭＡｂは、ＡＰＡＡＰ技法（（ｏｒｄｅｌ　ｌ
　ら：　Ｊ、　）Ｉｉｓｔｏｃｈｅｍ、　Ｃｙｔｏｃｈ
ｅｍ、　３２．２１９．１９８４）を用いて見出された
ように、冷温保存された（　ｃｒｙｏｐｒｅｓｅｒｖｅ
ｄ）組織上で正常ヒト組織と結合しない。したがって、
これらのＭＡｂをインビボで診断および治療に用いるこ
とが可能である。
用いるコンペティター（ｃｏｍｐｅｔｉ　ｔｏｒｓ）は
、キレ−）ＤＴＰＡおよびＥＤＴＡの非−複合および複
合型（付録１ｃ）である。
加えて、構造的に関連した化合物トランスアコニット酸
および１．２−ジアミノエタンをインヒビタ、−として
用いたく付録１ｅを参照されたい）。
ＭＡｂＢＷ２０５０／１７４はインビボ使用に特に適し
ており、池のＭＡｂ全てと対照的に、ＥＤＴＡ−Ｙへの
選択的結合を示す（付録１ｅ。
ＥＤＴＡ−Ｙの低いコンペティター過剰！（１００×）
と他のＥＤＴＡ複合体のより高い過剰量、を参照された
い〉。バイブリド２０５０／１７４を、したがって、安
定化させて、二特異性リセプターにおけるＥＤＴＡ−Ｙ
腕部を作出するのに用いた。
阻２±ＶｓｌａＣＨ１−リンカー−ＶＨ１ｂ　　Ｃｓ　
１遺伝子構築物の調製および発現 ここで用いた技法は、特に記載がない限り、Ｍｏ１ｅｃ
ｕｌａｒ　Ｃｌｏｎｉｎｇ、Ａ　Ｌａｂｏｒａｔｏｒｙ
　Ｍａｎｕａ１、Ｓａｍｂｒｏｏｋ、　　Ｆｒ１ｔｓｃ
ｈ、　　Ｍａｎｉａｔｉｓ、　　Ｃｏ１ｄ　　５ｐｒｉ
ｎ８ｔｌａｒｂｏｒ　Ｌａｂｏｒａｔｏｒｙ、　１９８
２　（ｐｐ、　１１−４４．５１−１２７．１３３−１
３４．１４１Ｓ１４６．１５０−１６７．１７０．１８
８−１９３、＋９７−１９９．２４８−２５５．２７０
−２９４．３１０−３２８．３６４−４０１．４３７−
５０６）およびＭｏ１ｅｃｕｌａｒ　Ｃｌｏｎｉｎｇ、
　ＡＬａｂｏｒａｔｏｒｙ　Ｍａｎｕａ１、５ｅｃｏｎ
ｄ　Ｅｄｉｔｉｏｎ、　Ｓａｍｂｒｏｏｋ。
Ｆｒ１ｔｓｃｈ、　Ｍａｎｉａｔｉｓ、　Ｃｏ１ｄ　Ｓ
ｐｒｉｎｇ　ＨａｒｂｏｒＬａｂｏｒａｔｏｒｙ　Ｐｒ
ｅｓｓ、　１９８９　（ｐｐ、１６．２−１６．２２．
１６．３０−１６．４０．１６．５４−１６．５５）か
ら採用した。
ヒトＩｇＣ；、Ｃ遺伝子を、ＥＭＢＬ３ファージ（Ａ、
Ｍ、　　Ｆｒ１ｓｃｈａｕｆ　　ら　：　　Ｊ、　　Ｍ
ｏ１．　　Ｂｉｏ１、　　１７０　、８２７−８４２．
１９８３およびＧ、Ｈ，Ａ、　Ｓｅｅｍａｎｎら：　Ｔ
ｈｅ　ＥＭＢＯＪｏｕｒｎａｌ　５．５４７−５５２．
１９８６）中のヒト遺伝子バンクから単離した。
一方でＣ，１エクソンおよびヒンジエクソンのみを含み
（第５図）、他方でＣＨ１エクソンおよびＨＬＡＢ２７
遺伝子の３°ＮＴ領域を含む（第６図、プラスミドＭ中
の断片Ｍ）、構築物をこのＩｇＧ、Ｃ遺伝子から独国特
許出願第Ｐ　３８２５６１５．０号明細書に記載のよう
にして調製した。
ＶＨａおよび■Ｈｂ遺伝子を、バイブリドクローンａお
よびｂのｍ　ＲＮ　Ａから０ｒｌａｎｄｉら（Ｐｒｏｃ
。
Ｎａｔ１、　Ａｃａｄ、　Ｓｃｉ、　ＵＳＡ　８６．３
８３３−３８３７．１９８９）による記載のようにして
増幅させて、Ｍ１３ベクター中でクローニングした（Ｖ
Ｈａ　　ＰＣＲおよびＶＨｂ　　ＰＣＲ）（第７図）。
■８ａ遺伝子をＨｉ　ｎ　ｄｍ−Ｂ　ａｍＨＩ断片とし
て真核細胞発現ベクターｐ　Ｅ　Ｖ）ｌ　（Ｓｉｍｏｎ
ら二Ｎｕｃ１、Ａｃ１ｄｓ　Ｒｅｓ。
１６．３５４．１９８８）中でクローニングした（第８
図）。
その結果、プラスミドｐＥＶＨａＣが得られた。
ＣＨｌおよび一つのヒンジエクソンを有するヒトｒｇＧ
ｃ遺伝子サブクローン（第５図）は、ＣＨ１エクソンと
ヒンジエクソンとの間にＰｓｔｌ切断部位を含む。■８
遺伝子は、５′末端にＰｓｔｌ切断部位を含む。リンカ
−オリゴヌクレオチドは、それが５′末端でＩｇＧＣ遺
伝子のＣＨ１＋ＩＨサブフラグメント上のＰｓｔＩ切断
部位領域および３゛末端でｖ、ｂ遺伝子のＰｓｔｌ切断
部位と、重複（ｏｖｅｒｌａｐ）するように設計されて
いる。リンカ−オリゴヌクレオチドは、そのＰｓｔＩ切
断部位によってＰＵＣ１８プラスミドのＰｓｔｌ切断部
位にクローニングされる（第９図）。結果としてプラス
ミドクローンＬが得られる。
ＣＨ１エクソンおよびヒンジエクソンを有するＩｇＣ；
３Ｃ遺伝子サブフラグメントを有するプラスミドを、Ｐ
ｓｔＩおよびＢａｍＨＩで切断して、Ｖ、４ｂＰＣＲか
らＰｓ　ｔ　Ｉ−ＢａｍＨＩ断片として切り出したＶＨ
ｂ遺伝子断片に連結させる（第１０図）。その結果、プ
ラスミドＸが得られる。
プラスミドＸをＰｓｔｌで切断して、プラスミドＬから
同様にＰｓｔｌで切り出しておいたリンカ−断片に連結
させる（第１１図）。核酸配列分析を用いて、リンカ−
が、正しい位置方向でＣ８ｌとｖＨｂとの間にイントロ
ン３とリンカ−エクソン間のイントロン／エクソン結合
部を損なわず、かつ、リンカ−とＶ。ｂ遺伝子間の結合
部における解読枠を損なわずにクローニングされている
、クローンＺを同定する。
プラスミドｐＥＶａ　ＣをＢａｍＨＩで切断して、プラ
スミドＭからＢａｍＨＩで切り出しておいた断片Ｍと連
結させる。制限酵素分析を用いて、断片Ｍを正しい位置
方向で含んでいるクローンＹを同定する（第１２図）。
プラスミドＹをＢａｍＨＩで部分的に切断して、全ての
末端を埋填した後に、プラスミドＸからＨｉｎｄＩＩＩ
およびＢａｍＨＩ切断によって切り出した断片（Ｃ□１
−リンカー−ｖ、ｂ）に連結する。ヌクレオチド配列分
析および制限地図作出を用いて、全てのエクソンを正し
い位置方向で有する融合遺伝子ＶＨａ　Ｃ，１−リンカ
ー−ｖＨｂ　　ｃ、ｉを含むブラスミドクローンＰＥＶ
Ｔを同定する（第１３図）。
プラスミドＰＥＶＴを、抗体ａ　Ｆ　（ａｂ）抗体ｂＦ
　（ａｂ）融合タンパク質を発現させるために、抗体ａ
およびｂの軽鎖の遺伝子を有するプラスミドとともに過
当な真核発現細胞にトランスフェクトさせる。
例」」−二つの異なるＭＡｂの軽鎖および重鎖遺伝子（
４遺伝子）のトランスフェクション免疫グロブリン遺伝
子の単離は、独国特許出願第Ｐ　３９０９７９９．４号
明細書に記載されている。
ベクターにクローニングされた遺伝子を、ベクターを線
状にした後にエレクトロポレーション（ｅｌｅｃｔｒｏ
ｐｏｒａｔｉｏｎ）によってＸ６３Ａｇ８．６５３ミエ
ローマ細胞（ｔＬ　５ｔｏｐｐｅｒら：Ｂｉｏｃｈｅｍ
、　Ｂｉｏｐｈｙｓ、　Ａｃｔａ　９００．３８−４４
．１９８７）中にトランスフェクトさせた。選択培地中
で増殖した形質転換体を、特異的ＲＩＡ中で二特異性−
価ＭＡｂの産生について試験した。このＲＩＡは、カゼ
インによる非特異的部位のブロックの後、分析される形
質転換体上清を上に位置させた同相上に吸着させたＴＡ
Ａからなった。９［ｌＹまたは９９１ＩＴｃと複合して
いるＤＴＰＡまたはＥＤＴＡを加えてから過剰分を洗い
流した後、二特異性−価抗−ＴＡＡＸ抗−ＥＤＴＡ　Ｍ
Ａｂを分泌したこれら形質転換体を、固相上の増加した
放射性シグナルによって検出することが可能であった。
形質転換体９を、制限希釈クローニングによって安定化
させて細胞培養中に広げた。細胞培養上清を、ＩＯＸに
濃縮して、ＭＡｂ画分をタンパク質Ａクロマトグラフィ
ー（Ｐ、Ｌ、　ｉ：、ｙら：ｍｍｕｎｏｃｈｅｍｉｓｔ
ｒｙ　１５．４２９．１９７８）によって精製し、二特
異性−価ＭＡｂを含む両分をアニオン交換クロマトグラ
フィー　（Ｊ、　Ｖａｎ　Ｄｉｊｋら：　Ｉｎｔ、　Ｊ
。
Ｃａｎｃｅｒ　４３．３４４−３４９．１９８９）によ
って精製した。
阻ユニ生物学的有効性 二特異性−価ＭＡｂ　（ＢＷ４３１．／２６ＸＢＷ２０
５０／１７４）を含む精製タンパク質を、５００μ８の
投与量で０．３．５．８．１０および１２日ＩＣヒトｌ
［異種移植片（ｘｅｎｏｇｒａｆ　ｔｓ）（ＣｏＣａ４
）を有するヌードマウスに静脈内注射した。２７〜３０
日目の各動物にＥＤＴＡ−Ｙ２Ｏの５０７１Ｃｉを静脈
内注射した。第二のグループの動物には同じ日に二特異
性ＭＡｂの代わりに５００　Ｉｔ　ｇのＭＡｂ　　ＢＷ
４３１／２６、およびＥＤＴＡ−Ｙ９０注射を上記のよ
うに行った。
第三の腫瘍を有するグループには、ＭＡｂおよびＥＤＴ
Ａ−Ｙ２Ｏの代わりにＰＢＳ（腫瘍増殖コントロールと
して）を注射した。腫瘍の増殖を６週間追跡した。ＥＤ
ＴＡ−Ｙ２Ｏの注射の結果、二特異性−価ＭＡｂを注射
されたグループにおいて１［の増殖の有意の阻害が認め
られたが、一方、ＭＡｂ　　ＢＷ４３１／２６を注射し
て、ＥＤＴＡ−Ｙ２Ｏで処理した動物では、ＰＢＳのみ
を注射された動物と同じく、腫瘍増殖の阻害がみられな
かった・ これらのデータは、毒性素因（ｐｒｉｎｃｉｐｌｅ）と
してＥＤＴＡ−Ｙ２Ｏと組合せて二特異性−価ＭＡｂの
選択的腫瘍治療効果を示す。
さらにより好ましい腫瘍治療効果は、オリゴ価／二特異
性またはオリゴ特異性リセプターによって得られる。な
ぜならば、これらはＴＡＡとの二価結合のために腫瘍上
により長く保持され、したがって、リガンドが同様に腫
瘍上により長く、より高濃度で保持されるからである。
畦５士抗−キレート腕部の強い要求性（ａｖｉｄｉｔｙ
）を増加させることによる、二特異性またはオリゴ特異
性巨大分子の生物学的有効性の最適化細胞外分布をして
いる親水性キレートのオリゴ特異性巨大分子の抗−キレ
ート腕部への効果的な付着に影響する決定的な因子は、
キレートへのこの腕部の強い要求性である。モノクロー
ナル抗体のそれらの対応するエピトープへの強い要求性
は、１０５〜１０１１１／ｍｏｌの範囲である。これら
の結合強度は、効果的なラジオイムノセラピー（ｒａｄ
ｉｏｉｍｍｕｎｏｔｈｅｒａｐｙ）に必要な量のキレー
トを腫瘍上に位置させるにはあるいは不十分であること
から、次の例においては、ｆｏｓ−ロイシン−ジッパ−
（ｚ　ｉ　ｐｐｅｒ）ペプチド（ｆｏｓ−ペプチド）と
ｊｕｎ−ロイシン−ジッパ−ペプチド（ｊｕｎ−ペプチ
ド）　　（Ｅｒｉｎに、　Ｏ’５ｈｅｒａら：　５ｃｉ
ｅｎｃｅ、　２４５、１９８９）とのきわめて強い相互
作用を用いて、キレートをできるだけ強固に抗−キレー
ト腕部上に固定化した。この強力なｆｏｓ−ｊｕｎ相互
作用を利用することができるように、好ましくは、ｆｏ
ｓ−ペプチドを共有結合でキレート（ＤＴＰＡ）に連結
させることが必要である。この目的のために、第一の手
段においてイソチオシアネートベンジル−ＤＴＰＡをヒ
ドラジン（またはジアミノアルカン）と反応させること
が可能である。このようにして産生されたＤＴＰＡ−ベ
ンジルチオカルバジドを、第二段階において、Ｎ−（γ
−マレイミドブチリルオキシ）サクシニミドまたは類似
体と反応させて、ＤＴＰＡ−ベンジル−（γ−マレイミ
ドブチリル）チオカルバジドを得ることができる。次い
で、第三の段階で、この化合物をグリシン−グリシン−
システィン（第１図）によって広げておいたｆｏｓ−ペ
プチドに、アミノ末端のシスティンの遊離のＳＨ基を介
して連結させる。このようにして産生されたｆｏｓ−ペ
プチド−ＤＴＰＡ抱合体（ｃｏｎｊｕｇａｔｅ）を、第
四段階において、塩化イツトリウム（ｙｔｔｒｉｕｍ）
と複合化させる。このようにして産生されたｆｏｓ−ペ
プチド−ＤＴＰＡ−Ｙ抱合複合体を、次いでニーまたは
オリゴ特異性巨大分子のｊｕｎ−ペプチド腕部へのイン
ビボ添加に用いることができる。以上略述した例の合成
を以下に詳述する。
イソチオシアネートベンジル−ＥＤＴＡ　（ＳＣＮ−Ｂ
ｎ−ＥＤＴＡ）　（３０ｍｇ、　５４μｍｏｌ）を１０
％（Ｖ／Ｖ）水成ヒドラジン中で１時間攪拌した。次い
で、溶媒を高真空下で除去して、残留物を五酸化リン上
で高真空下で乾燥させて、最後に凍結乾燥した。産生物
をＤＯ讐ＥＸ讐Ｘ　２　（Ｈ”型）で中和して、再び凍
結乾燥した（収！２８ｍｇ）。
段階１で調製されたＥＤＴＡ−ベンジルチオカルバジド
（２０ｍｇ、３４μｍｏｌ）およびＮ−（ｒ−マレイミ
ドブチリルオキシ）サクシニミド（８ｍ８．２９μｍｏ
ｌ＝０．９等量）を無水ジメチルフォルムアミド中で１
時間攪拌した。混合物を、次いで、蒸発させて乾燥して
、残留物を高真空下で乾燥した。
ｆｏｓ−ペプチド（４，８ｍｇ、　　１７１ｍｏｌ）（
段階３．１を参照されたい）の燐酸緩衝生理食塩水（２
ｍｌ）を、段階２で得られた産生物混合物（４ｍｇ）の
ジメチルフォルムアミド（４００μｍ）懸濁液と混合し
て、室温で１時間インキュベートした。反応混合物を、
次いで、燐酸緩衝生理食塩水中でセファデックス０１５
カラム上でのゲル濾過に供した。
タンパク質を含む溶出液を集めて一３０℃で保存した（
収ｆ１４．２ｍｇ）。
段階３，１： Ｎ−末端ＧＧＣ延長を有するｆｏｓ−ペプチド（１１）
のアミノ酸配列 各アルファベット文字は次のアミノ酸を表す。
Ａ＝アラニン、Ｃ＝システィン、Ｄ＝アスパラギン酸、
Ｅ＝グルタミン酸、Ｇ＝ニブリシン■＝イソロイシン、
Ｋ＝リジン、Ｌ＝ロイシン、Ｍ＝メチオニン、Ｎ＝アス
パラギン、Ｑ＝グルタミン、Ｒ＝アルギニン、Ｓ＝セリ
ン、Ｔ＝スレオニン、■＝バリン、Ｙ＝チロシン。
オリゴペプチドを、自動ペプチド合成機（Ａｐｐｌｉｅ
ｄ　Ｂｉｏｓｙｓｔｅｍｓ　Ｍｏｄｅｌ　４３０Ａ）を
用いてタート−ブチルオキシカルボニル保護基を用いる
Ｍｅｒｒｉｆｉｅｌｄ固相法（ＳｔｅｗａｒｔおよびＹ
ｏｕｎ８：５ｏｌｉｄ　Ｐｈａｓｅ　５ｙｎｔｈｅｓｉ
ｓ％Ｐｉｅｒｃｅ　Ｃｈｅｍｉｃａｌ（ｏｍｐａｎｙ、
第二板Ｒｏｃｋｆｏｒｄ　’Ｉ１１．）によって合成し
た。オリゴペプチドを、フェニルアセタミドメチル−ポ
リスチレン支持体から切り出した。保護基（Ｔｏｍら：
　Ｊ、　Ａｍ、　Ｃｈｅｍ、　Ｓｏｃ、　１０５．６４
４２−６４５５、＋９８３）を除去した後、オリゴペプ
チドをＲｉｖｉｅｒら（Ｊ、　Ｃｈｒｏｍａｔｏｇｒａ
ｐｈｙ　２８８．３０３−３２８．１９８４）による記
載の逆相クロマトグラフィー（ＰｅｐＲＰＣカラム、Ｐ
ｈａｒｍａｃｉａ社製）によって精製した。
段階３のようにして調製されたｆｏｓ−ペプチド−ＥＤ
ＴＡ抱合体（４，２ｍｇ）を、等張生理食塩水１０．１
Ｍクエン酸ナトリウム（ｐＨ７，０）に対して、分子ｆ
ｌ１、０００の排除限界（ｅｘｃｌｕｓｉｏｎｌｉｍｉ
ｔ）を有する透析チューブ（スペクトラム）中で透析し
て、３ｍｌの等張生理食塩水１０．１Ｍクエン酸ナトリ
ウム（ｐＨ７，０）に溶解した６ｍｇの塩化イツトリウ
ムと混合した。１時間後、燐酸緩衝生理食塩水に対して
逆透析を行って、キレート溶液を一３０℃で保存した。
上記の例ζこ記載したｆｏｓ−ペプチド−ＥＤＴＡ−イ
ツトリウムキレートを次いｔ、°高い要求性で二特異性
またはオリゴ：特異性巨大分子のｊｕｎ−ペプチド腕部
と結合させるために、リガンドとして用いる。特にこの
相互作用に適している二特異性巨大分子の構築は、次の
例に記載されている。
Ｂ）　　　−八 ここで用いる技法は、特に記載がない限り、Ｍａｎｉａ
ｔｉｓら　（Ｌａｂｏｒａｔｏｒｙ　Ｍａｎｕａｌ　　
ＥＭＢＬ、　　１９８２、Ｈｅ１ｄｅｌｂｅｒ：ｇ）お
よびＳａｍｂｒｏｏｋ　（ＭｏｌｅｃｕｌａｒＣｌｏｎ
ｉｎｇ：　Ａ　Ｌａｂｏｒａｔｏｒｙ　Ｍａｎｕａｌ）
から採用した。
丞！ユ± ヒトｒｇｃ３ｃ遺伝子を、ＥＭＢＬ３ファージ（Ａ、Ｍ
、　Ｆｒ１ｓｃｈａｕｆら：　Ｊ、　Ｍｏ１．　Ｂｉｏ
１、　１７０．８２７−８４２．１９８３およびＧ、Ｈ
，Ａ、　Ｓｅｅｍａｎｎら：　Ｔｈｅ　ＥＭＢＯＪｏｕ
ｒｎａｌ　５．５４７−５５２．１９８６）中のヒト遺
伝子バンクから単離した。１ｇＧ３Ｃ遺伝子のＣＨＩエ
クソンおよび最初のヒンジエクソンのみを含む構築物（
Ｄ）（第１４図）を、この１ｇＧ３Ｃ遺伝子から独国特
許出願第Ｐ　３Ｂ２５６１５．０号明細書に記載のよう
にして調製した。
ヒ）ＨＬＡ　Ｂ２７に遺伝子を、同じ遺伝子バンクから
同じく独国特許出願第Ｐ　３８２５６１５．０号明細書
に記載のようにして調製した。Ｃ３エクソンおよびＨＬ
Ａ　Ｂ２７に遺伝子の３’　ＮＴ領領域みを含む構築物
（Ｅ）（第１５図）を、このＨＬＡ　Ｂ２７に遺伝子か
ら調製した。
旦匿ユ± Ｃ１エクソンおよびＨＬＡＢ２７に遺伝子の３’　ＮＴ
Ｖｉ域をプラスミドＥからＸｂａｌで切り出して、断片
を単離して、構築物りのＸｂａＩ切断部位にクローニン
グした。制限酵素分析および核酸配列分析を用いて、Ｃ
３エクソンおよびＨＬＡ　Ｂ２７に遺伝子の３’　ＮＴ
領領域正しい５’−３’の位置方向で含む、３′がＩｇ
Ｇ３Ｃ遺伝子断片からである、クローンＦを同定した（
第１６図）。
濃遭λユ クローンＦの挿入物を、エンドヌクレアーゼＨｉ　ｎｄ
ｍおよびＥｃｏＲＩを用いてプラスミドから切り出して
、Ｍ１３ｍｐ１８二本鎖（ＤＳ）ファージのＨｉｎｄｍ
とＥｃｏＲＩ切断部位切断部位−ニングする。抗体／Ｈ
ＬＡ融合遺伝子断片を含むファージクローンＧを単離す
る（第１７図）。
貝！Ａ± ウラシル−末鎖を、ファージクローンＧからＴ。
Ａ、　Ｋｕｎｋｅｌ　（Ｐｒｏｃ、　Ｎａｔｌ。Ａｃａ
ｄ、　５ｃｉｅｎｃｅ、　Ｕ、Ｓ、Ａ。
８２．４８Ｂ−４９２，１９８５）の方法で調製する。
−末鎖ファージを、突然変異誘導性（ｍｕｔａｇｅｎｉ
ｃ）オリゴヌクレオチド１および２（表６）とハイブリ
ダイズさせて、オリゴヌクレオチド間の間隙をフレノウ
ＤＮＡポリメラーゼおよびＴ４リガーゼで閉環させた。
大ＫＭ　（Ｅ、　ｃｏｌｉ）中での形質転換の後、制限
酵素分析および核酸配列分析を用いて、ヒンジエクソン
の５′末端における５ｓｔｌ制限酵素切断部位が除去さ
れたファージクローン（Ｇ）を同定した。同時に、５ｓ
ｔＩおよび５ｐｈＩ制限酵素切断部位を、ヒンジエクソ
ンの３′末端に導入したく第１８図）。５ｓｔＩ切断部
位を除去するためにヒンジエクソンの第二のコドンの３
番目の塩基をＣからＧに変換して、５ｓｔＩおよび５ｐ
ｈＩ切断部位を導入するために塩基群５　’　ＧＡＧＣ
ＴＣＧＧＧＧＣＡ３　’をヒンジエクソンの１５番目と
１６番目のコドンの間に導入したく表７）。
戊ｌ五上 ファージクローンＧ′の二本鎖ＤＮＡを、ｓｐｈ　Ｉで
完全に５ｓｔｌで部分的に切断する。
合成オリゴヌクレオチドＪｕｎＩおよびＪｕｎ［Ｉ（表
８）を合わせて、その各末端に５ｐｈｌおよび５ｓｔＩ
制限酵素切断部位の切断部を含み、Ｊｕｎロイシンジッ
パ−（０’５ｈｅａら：　５ｃｉｅｎｃｅ。
２４５．６４６−６４８．１９８９）を含むペプチドを
コードする、二本鎖ＤＮＡ断片が得られる。
二本鎖ＤＮＡ断片をＦ′ファージクローンの５ｓｔＩお
よびｓｐｈ　Ｉ制限酵素切断部位にクローニングして、
ヒンジエクソン中にＪ　ｕ　ｎジッパ−ペプチドのため
の配列が挿入された遺伝子構造物を含むファージクロー
ンＨな同定する（第１９図）。
旦及玉士 ＤＳファージＨの挿入物を、制限エンドヌクレアーゼＨ
ｉｎｄｌＩＩおよびＥｃｏＲＩで切り出して、末端をＴ
４ポリメラーゼで埋填して、ＳｍａＩ−切断ＫｓＦベク
ター（Ｓｔｒａｔａ３ｅｎｅ、　１１０９９　Ｎｏｒｔ
ｈＴｏｒｒｅｙ　Ｐｉｎｅｓ　Ｒｏａｄ％Ｌａ　Ｊｏｌ
ｌａ　Ｃａ１ｉｆｏｒｎｉａ　９２０３７）中にクロー
ニングした。抗体／Ｊｕｎ／ＨＬＡ融合遺伝子をその両
側をＢａｍＨＩ切断部位で挟むように位置して含む、プ
ラスミドクローンｌを同定した（第２０図）。
丞監ユ± 抗体／Ｊｕｎ／ＨＬＡＭ合遺伝子を、Ｋ　ＳクローンＩ
からＢａｍＨＩで切り出して、特異的機能性免疫グロブ
リン■遺伝子を含む発現プラスミドｐ　Ａ　Ｂ　Ｓ　ｔ
　ｏ　ｐ　（Ｂｅｈｒｉｎｇｗｅｒｋｅ　ＡＧ）中にク
ローニングした。特異的■遺伝子を、特許出願第Ｐ、３
９０９７９９．４号明細書に記載のようにして得る。抗
体／Ｊｕｎ／ＨＬＡ！合遺伝子構築物を正しい位置方向
でｖＨ遺伝子の下流に含む発現プラスミドＫを、同定し
た（第２１図）。
プラスミドにと特異的ＭＡｂの軽鎖のための遺伝子を含
むプラスミドおよび耐性（ｒｅｓｉｓｔａｎｃｅ）遺伝
子を有するプラスミドの共形質転換（ｃｏｔｒａｎｓｆ
ｏｒｍａｔｉｏｎ）によって、ヒンジ領域に二つのＪｕ
ｎジッパ−ペプチドを含み、もはやいかなるホモダイマ
ー（ｈｏｍｏｄｉｍｅｒ）　　（Ｊ　ｕ　ｎ　／　Ｊ　
ｕ　ｎ）形成のないようにＪｕｎジッパ−ペプチドが修
飾されている、特異的抗体Ｆ　（ａｂ’）　２断片の発
現が導かれる。
他者による科学的な研究調査は、巨大分子（＞５０ｋＤ
ａ）による固体腫瘍の浸透（ｐｅｎｅｔｒａｔｉｏｎ）
は援慢に起き、通常、縁辺領域または腫瘍の少ない領域
のみに達することを示している。これらの研究調査は、
少量の巨大分子の一回の注射からなる実験に基づいてい
る。これに対して、本発明者らは、ヌードマウス異種移
植片における全腫瘍体の実質的な侵透が多量の二特異性
またはオリゴ特異性リセブターの反復的な静脈内注射（
１０Ｘ２５０μｇリセブター／マウス、１０日間）によ
って可能であることを見、出した。さらに、これら′の
ＴＡＡへの特異的結合の故に二特異性またはオリゴ特異
性リセブターは、腫瘍細胞膜上および腫瘍間隙中で長期
の開く〉２０日）大量に付着したままで保持される。こ
れらの結果は、ヒト直腸および膵臓腫瘍異種移植片の冷
温保存された（　ｃｒｙｏｐｒｅｓｅｒｖｅｄ）薄切片
に間接的アルカリフォスファターゼ技法を用いて得られ
た。
この間（わずか１０日後）に二特異性およびオリゴ特異
性リセブター分子は、崩壊および排除によってＴＡＡ−
陰性正常組織および血液から既に除去されていた。この
除去期間を短縮するために非結合の二特異性またはオリ
ゴ特異性リセブター分子の抗−ＴＡＡ腕部とのみ反応す
る抗−イディオタイプＭＡｂ（抗Ｉｄ）をニーまたはオ
リゴ特異性リセブターの１０回の注射の完了後２４時間
に静脈内注射した。この−回の注射は、非結合ニーまた
はオリゴ特異性リセブター分子の血液からの除去を速め
て、肝臓および牌臓における代謝率を高めた。
この操作に基づいて、キレ−）　（ＥＤＴ八−Ｙ２Ｏ）
をニーまたはオリゴ特異性リセブターの浸透および結合
相の完了後わずか４日後に注射することが可能である。
次の治療方法（ヌードマウス用）は、これらの知見から
導かれたものである。
ａ）　１〜１０日目、各回ｌＸ２５０μｇのニーまたは
オリゴ特異性リセブターの静脈内注射ｂ）　１１日ｎ１
１×５０μｇの抗１ｄの静脈内注射 ｃ）　　１４日ｌ１治療的投与量のＥＤＴＡ−Ｙ２Ｏの
静脈内注射 ヌードマウスと腫瘍患者における比較的免疫シンチグラ
フ（ｉｍｍｕｎｏｓｃｉｎｔｉｇｒａｐｈｉｃ）データ
に基づいて、この方法は、ヒトにおいても腫瘍治療に適
していると考えられる。しかし、ヒト系において注射さ
れるべき量は、範囲が異なる（１０Ｘ５〜１０ｇの二特
異性すセブタ−ｌＸ１ｇの抗Ｉｄ）。抗１ｄの注射は、
治療には必ずしも必須ではない。
材料二分割可能な９６−ウェルポリスチレンマイクロタ
イタープレート（Ｕ型）タイプＢ、　Ｎｕｎｃ社製、Ｎ
ｏ、４−６０４４５ １）　　１．＋１ｇ抱合体／ｍｌＰ　Ｂ　Ｓ　（ｐ　Ｈ
７，２）の濃度の５０μｌのＹ−ベンジル−ＤＴＰＡ−
Ｈ９Ａ１９抱合体を、各ウェルにピペットで入れて、室
温で一晩インキユベートする。
２）　上清を吸引によって取り除いて、３回０．０５Ｍ
）リスクエン酸塩緩衝液（ｐＨ７，４）（洗浄溶液１）
で洗浄する（１回洗浄＝２５０μｍ／ウェルの洗浄液を
ウェルに入れて２分間静置してから吸引によ）て除去す
る）。
３）　マイクロタイタープレートがすぐに必要でない場
合には、それをセルロース上に室温で一装置く（開口部
を下にして）。次いでプレートを、乾燥カートリッジ（
Ｇａｐｌａｓｔ社製、Ｐｏ５ｔｒａｃｈ　５２９．８１
００　Ｇａｒｍｉｓｃｈ−Ｐａｒｔｅｎｋｉｒｃｈｅｎ
）とともにフィルムに密閉する。プレートを、＋４℃で
これらの条件下で少なくとも８週間保存することができ
る。
４　）　　２５０　ｔｔ　ｌのブロッキング溶液を各ウ
ェルに入れて、３７℃で３０分間インキュベートする。
５）　希釈されたハイブリドーマ上清とコンペティター
との予備インキュベーションをブロッキングの開に行う
（付録２を参照されたい）。
６）　５０μｍの適宜に予備希釈して予備インキュベー
トした試験すべきハイブリドーマ上清を、各ウェルζこ
入れて、室温で３０分間インキニーベートする。
７）　洗浄溶液２で３回洗浄を続いて行う。
８）　次いで、アルカリフォスファターゼで標識してか
らブロッキング溶液て１：５００に希釈しておいたヤギ
抗−マウスＩ　ｇＧ、抗体５０　／ｌＩを各ウェルに入
れて、室温で３０分間インキュベートする。
９）　次いで、Ｅｎｚｙｇｎｏｓｔのための洗浄溶液で
３回洗浄を行う。
１０）　次いで、５０μｍの０．１ｍＭＮＡＤＰを加え
る。
１１）　室温でのインキュベーションを次いで３０分間
行う。
１２）　　ＮＡＤＰどのインキュベーションの間に、増
幅系を次のようにして作る。
プレート当り２部のＩＮＴとＩＢのＰＢＳ（ｐＨ７，２
）を混合して、１部のジアホラーゼ（ｄ　１ａｐｈｏｒ
ａｓｅ）と１部のＡＤＨをピペットで入れる。
１３）　この系の５０１ｔ　！を各ウェルに入れる。
１４）　透明から赤へと色に明確な変化が起きたとき、
ウェル当り１００μｍのＯｏｌ　ＮＨ２ＳＯ４溶液によ
って反応を停止させる。
１５　）ＴＩＴＥＲＴＥＫＲＭＵＬＴＩＳＣＡＮ中で４
９２　ｒｕｎで吸光度（ｅｘｔｉｎｃｔｉｏｎ）を測定
する。５０μｍのＮＡＤＰと５０μｍの溶液および１２
００μｍの０．１　ＮＨ２ＳＯ４をブランクとして用い
る。
ＮＡＤＰ ＩＮＴ ＡＤＨ ＤＩＡＰＨＯＲＡＳＥ 洗浄液２ シグマ注文番号Ｎ−０５０５ シグマ注文番号１−８３７７ シグマ注文番号Ａ−３２６３ シグマ注文番号ｄ−２３８１ ベーリング注文番号ＯＳＥＷ９６ Ｔｗｅｅｎ／ＰＢＳを含む ブロッキング溶液： ＰＢＳ　（ｐＨ７，２）に、カゼインを加えて３０分間
攪拌してカゼイン３％濃度にして、ｐＨを７．４に調整
する。次いで４．ＯＯＯｒｐｍで１０分間遠心分離して
粒子を除去する。
希釈ヤギ抗−マウスＩ　ｇｃ、抗体をアルカリフォスフ
ァターゼ（Ｓｏｕｔｈｅｒｎ　Ｂｉｏｔｅｃｈｎｏｌｏ
ｇｙＡｓｓｏｃｉａｔｅｓ社製、カタログ番号１０８０
−０４）で標識する。
０．１ｍＭＮＡＤＰの調製ニ ア、６５ｍｇのＮＡＤＰを、１００ｍ１の２０ｍＭ）リ
ス、０　、１　ｍＭ　Ｍ　ｇ　Ｓ　Ｏａ　（ｐＨ９，５
）に溶解する。
この溶液は一２０°Ｃで数カ月保存できる。
Ｉ　Ｎ　Ｔ　（Ｐ−ＩＯＤＯＮＩＴＲＯＴＥＴＲＡＺＯ
ＬＩＵＭ　Ｖｉｏｌｅｔ）の調製：２　、５　ｍｇ／ｍ
ｌの３０％エタノールを超音波槽で溶解する。常に新鮮
なものを調製する。
ジアホラーゼの調製： １Ｂジアホラ一ゼ／ｍｌＰ　Ｂ　Ｓ　（ｐ　Ｈ７，２）
を少量づつに分けて一２０℃で保存する。
アルコールデヒドロゲナーゼの調製： ０−５ｍｇＡＤＨ／ｍ１ＰＢｓ　（ｐＨ７，２）を少量
づつに分けて一２０℃で保存する。
ハイブリドーマ上清中のマウスＩ　ｇＣ；８度を、市販
の定量ＥＬＩＳＡ系を用いて決定することができる。
ＥＬＩＳ／”１度決定に基づいて、ハイブリドーマ上清
をＣａ”およびＭｇ″″′″を含まないＰＢＳ中で１．
２５７１３／ｍｌに希釈する。
ダラムからモル（ｍｏｌ）への変換： １５０．０００ｇ　　　−１モルのＭＡｂｌ　、２５Ｘ
　１０−６ｇ　　−ｘモル１．２５μｇ　　　　　＝ｘ
＝８．３３Ｘ４０−１２モルＭＡｂとインヒビターの１
＋１比を得るために、８．３３Ｘ　１０−１２モル／２
００μｍ（これは５の係数（ｆａｃｔｏｒ）で増える）
の濃度のインヒビターの１０　）ｉ　ｌを、８．３３Ｘ
　１０−’２モル／ｍｌの濃度のハイブリドーマ上清の
５０　／Ｚ　ｌに加える。
ハイブリドーマ上清を、コンペティターの１００．００
０倍、５０，０００倍、１０，０００倍、５．０００倍
、１，０００倍および１００倍の濃度で室温で３０分間
インキュベートする。この５０μ＋を、ピペットでＥＬ
ＩＳＡ、（付録１ａのｎｏ。
６を参照されたい）に入れる。
−はハイブリドーマ上清中に含まれるＭＡｂの１００．
０００倍過剰となる。より低いコンペティターとＭＡｂ
比は、コンペティター溶液を特別な塩イオン溶液で所望
のモル過剰に適宜に希釈することによって達成された（
付録１ｂを参照されたい）。
表Ｉに示したＤＴＰＡまたはＥＤＴＡの金属イオンとの
複合定数は著しく高いために、これら金属イオンとのＤ
ＴＰＡまたはＥＤＴＡの等モル混合では完全な飽和が期
待されねばならない。このために、対応する金属イオン
を、ＤＴＰＡまたはＥＤＴＡと３倍モル過剰量でインキ
ュベートした。
例として、１７０μｍの１０ｍＭ硫酸カドミウム溶液（
二度蒸留水溶液）（付録１ｄを参照されたい）を３０μ
ｍの１０２８モルＤＴＰＡ保存溶液（二度蒸留水溶液）
と室温で５分間インキュベートした。このコンペティタ
ー溶液１０　／１１をバイブリドーマ上清と混合するこ
とによって、コンベティタ硫酸カドミウム Ｒｉｅｄｅｌ　　ｄｅ　　）Ｉａｅｎ 塩化亜鉛 メルク社製 次の金属イオンの１０ミリモル溶液を、二度蒸留水中に
調製した。
塩化マンガン メルク社製 分子量　１６１．８８ Ｎｏ、　　５９３４ Ｍｎイオン半径：８０ｐｍ 分子量　２５６．５ Ｎｏ、　３１１４５ Ｃｄイオン半径：９７ｐｍ 分子ｆｉ　　１３６．２８ Ｎｏ、　８８１６ Ｚｎイオン半径ニア４ｐｍ 硫酸鋼 Ｒｉｅｄｅｌ ａｅｎ 塩化イッテリウム Ａｌｄｒｉｃｈ 硝酸（ＩＩ） １ｅｄｅｌ ａｅｎ 分子量　１５９．６１ Ｎｏ、　　３１２９４ Ｃｕイオン半径：９６ｐｍ 分子量　３０３．３６ Ｎｏ、　２０．４９１９ Ｙイオン半径：９２ｐｍ 分子量　３３１．２Ｏ Ｎｏ、　　３１１３７ ｐｂイオン半径：１２０ｐｍ 同相抗原との結合の５０％阻害を起こすコンペティター
の過剰モル ＭＡｂ　Ｎｏ＋ ２０５０／１７４ ２０５０１５３１ ２０５０１５３２ ２０５０１５３４ ２０５０１５３５ ＭＡｂ　Ｎｏ。
２０５０１５３１ ２０５０１５３２ ２０５０１５３４ ２０５０１５３５ ＭＡｂ　Ｎｏ。
２０５０／１７４ ２０５０１５３１ ２０５０１５３２ ２０５０１５３４ ２０５０１５３５ ＤＴＰＡ−Ｙ　ＤＴＰＡ　ＤＴＰＡ−Ｍｎ１０’　　　
　１０”　　１０” ５ｘｌＯ’　　１０３１０２ ５ｘｌＯ’　　１０３１０” ５ｘｌＯ’　　１０”　　１０” １０’　　　　１０”　　１０” ＤＴＰＡ−Ｃｄ　　ＤＴＰＡ−Ｚｎ １０”　　　　５ｘｌＯ３ １０”　　　　５ｘ１０３ １０”　　　　５ｘｌＯ３ １０”　　　　５ｘｌＯ３ １０”　　　　１０３ ＤＴＰＡ−Ｃｕ ｘｌＯ３ ５ｘｌＯ’ ｘｌＯ３ ｘｌＯ３ ０３ ＤＴＰＡ−Ｐｂ　　　１、スー　シ′７ミノ　　トラン
ス−１９ン　　　　　　　　７コ；７トゐ１ＤＴＡ−Ｙ ＥＤＴＡ−にｎ ７Ｊし 了Ｊし ｘｌＯ３ ５ｘｌＯ” ５ｘｌＯ” ０３ ＥＤＴＡ−Ｃｕ ０３ ０２ ｘｌＯ３ ０３ ０２ ＥＤＴＡ−Ｐｂ Ｘ１０３ １０’ １０’ ｘｌＯ３ ０２ ＤＴＰＡ 州曝
【図面の簡単な説明】
第１図および第３図は、重鎮遺伝子部分のポリペプチド
スペーサーによる結合構造を示す説明図ろる。 １２図および第４図は、それぞれ第１図および３図のも
のに軽鎖が対合した構造を示す説明図）る。 第５図〜第１３図はＶｌｌａＣＨｌ−リンカ−Ｖ）ｌｌ
ｂｃＨ１遺伝子構築物の構築を示す説明図である。 第１４図〜第２１図はＭａｂ−ｊｕｎ融合分子のための
プラスミドにの構築を示す説明図である。

Claims (1)

  1. 【特許請求の範囲】 １、二つまたはそれ以上の異なる特異性の抗体のＶ＿Ｈ
    およびＣ＿Ｈ１領域をコードするＤＮＡの過当なリンカ
    ーによる融合およびそれらに属する軽鎖のための遺伝子
    部分と合わせての発現系における続いての発現による遺
    伝子操作によって、得ることができる、二特異性または
    オリゴ特異性の一価またはオリゴ価リセプター ２、一つの特異性が動物またはヒト腫瘍関連抗原に対し
    て向けられている、請求項１に記載のリセプター。 ３、一つの特異性が触媒的または酵素的活性を有する、
    請求項１に記載のリセプター。 ４、一つの特異性が動物またはヒト腫瘍関連抗原に対し
    て向けられており、他の一つの特異性がキレートに向け
    られている、請求項１に記載のリセプター。 ５、キレート結合がｆｏｓ−ｊｕｎ相互作用を介してリ
    セプターキレート腕部で起きる、請求項４に記載のリセ
    プター。 ６、一つの特異性が表２、３、４または５に示される可
    変領域を有するモノクローナル抗体に由来する、請求項
    １、２、４または５に記載のリセプター。 ７、三つの結合部位が二つの特異性の場合に存在する、
    請求項１、２、４、５または６に記載のリセプター。 ８、四つの結合部位が二つの特異性の場合に存在する、
    請求項１、２、４、５または６に記載のリセプター。 ９、三つの特異性の場合、一つが腫瘍に向けられて、他
    の二つが異なるやり方でＤＴＰＡまたはＥＤＴＡに向け
    られている、請求項１、２、４、５または６に記載のリ
    セプター。１０、重鎖抗体部分をコードするＤＮＡ断片
    を　リンカーを用いて連結して、軽鎖のための遺伝子　
    とともに発現系で発現することからなる、請求項　１、
    ２、３、４、５または６に記載のリセプター　の製造法
    。 １１、医薬物としての、請求項１〜９のいずれ　か１項
    に記載のリセプター。　
JP2165485A 1989-06-22 1990-06-22 二特異性およびオリゴ特異性の一価およびオリゴ価リセプター、それらの調整および使用 Expired - Lifetime JP2978210B2 (ja)

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DE3920358.1 1989-06-22

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GR3021109T3 (en) 1996-12-31
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ATE142230T1 (de) 1996-09-15
EP0404097A2 (de) 1990-12-27
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PT94443B (pt) 1997-02-28
JP2978210B2 (ja) 1999-11-15

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