JPH0373280B2 - - Google Patents

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Publication number
JPH0373280B2
JPH0373280B2 JP59169370A JP16937084A JPH0373280B2 JP H0373280 B2 JPH0373280 B2 JP H0373280B2 JP 59169370 A JP59169370 A JP 59169370A JP 16937084 A JP16937084 A JP 16937084A JP H0373280 B2 JPH0373280 B2 JP H0373280B2
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Prior art keywords
cells
human
dna
producing
antibody
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JPS6147500A (ja
Inventor
Katsu Taniguchi
Yoshikazu Kurosawa
Kozo Sugita
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Shingijutsu Kaihatsu Jigyodan
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Shingijutsu Kaihatsu Jigyodan
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First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=15885326&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=JPH0373280(B2) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.
Application filed by Shingijutsu Kaihatsu Jigyodan filed Critical Shingijutsu Kaihatsu Jigyodan
Priority to JP16937084A priority Critical patent/JPS6147500A/ja
Priority to DE19853587360 priority patent/DE3587360T2/de
Priority to DE1985102665 priority patent/DE171496T1/de
Priority to EP85102665A priority patent/EP0171496B1/en
Priority to CA 476731 priority patent/CA1339201C/en
Publication of JPS6147500A publication Critical patent/JPS6147500A/ja
Publication of JPH0373280B2 publication Critical patent/JPH0373280B2/ja
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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
    • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
    • C07K16/28—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
    • C07K16/30—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants from tumour cells
    • C07K16/3053—Skin, nerves, brain
    • A—HUMAN NECESSITIES
    • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00—Medicinal preparations containing peptides
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2317/00—Immunoglobulins specific features
    • C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
    • C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K2319/00—Fusion polypeptide

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  • Health & Medical Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Immunology (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Cell Biology (AREA)
  • Medicinal Chemistry (AREA)
  • Biomedical Technology (AREA)
  • Biochemistry (AREA)
  • Biophysics (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Neurology (AREA)
  • Molecular Biology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Engineering & Computer Science (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
  • Peptides Or Proteins (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)

Description

【発明の詳細な説明】 本発明はキメラモノクナロール抗体及びその製
造法に関し、特に人体に投与した場合にアナフイ
ラキシーシヨツクや血清病などの副作用の少ない
モノクナロール抗体及びその製造法に関する。 単一抗原決定基だけを認識するモノクローナル
抗体は免疫学全体に大きな影響を与え、その有用
性は医学界にとゞまらず生物学、薬学、化学など
の多くの分野で証明されている。そして、このモ
ノクローナル抗体を得る方法に関しては1975年
Ko¨hlerとMilsteinがヒツジ赤血球で免疫したマ
ウスの脾細胞とマウスミエローマ細胞とを細胞融
合させることで実現し（Nature256495−497
（1975））、この外エプスタイン−バール（Epstein
−Barr）ウイルスによる方法などがある（特開
昭58−201723号参照）。しかして、これらのモノ
クローナル抗体の多くはそれ自体がマウス等人間
以外の動物に由来するためそれを人間に投与した
場合には異種蛋白を注射することになり、その結
果、アナフイラキシーシヨツクや血清病などの副
作用がおこることが予想される。そのため、ヒト
ハイブリドーマを用いてヒトモノクローナル抗体
を作成する試みがなされている。 （例えば特開昭57−126424号、特公表昭57−
502090号及び特開昭58−128323号参照）これらに
よればヒト型のモノクローナル抗体を得ることは
可能であるが必ずしも再現性等の点において満足
すべきものとは云えない。（Nature300316−317
（1982）参照） また、マウス等の動物は用意に種々の抗原で免
疫することは可能であるが人間については望む抗
原を用いて自由に免疫できないという欠点があ
る。一方、ヒト型モノクローナル抗体を生産する
ヒトＸマウスハイブリドーマを作製してμ鎖特異
的mRNAを得たのち相補鎖DNAを作製し、プラ
スミドpBR322に組み込んで大腸菌にヒトモノク
ローナル抗体を生産させる試みを行つているがこ
の方法も人間には自由に免疫できないという点で
問題が残る。 本発明者はこれらの欠点を改善すべく種々の研
究を行い本発明を完成するに至つたのである。す
なわち本発明はヒト以外の動物由来の可変領域と
ヒト由来の定常領域からなるキメラモノクローナ
ル抗体であつて、これの製造方法はヒト以外の動
物の抗体生産細胞のDNAから単離した活性なVH
とVL遺伝子、及び、ヒトDNAから単離したCHと
CL遺伝子を、VLの下流にCLを、VHの下流にCHを
それぞれ配列して発現ベクターに挿入し、該発現
ベクターを動物培養細胞に導入してキメラモノク
ロナール抗体を産生させることからなる。ここで
“活性なVHとVL遺伝子”とは抗体産生細胞におい
てDNAの配合列によつて出来たVHにあつてはＶ
−Ｄ−Ｊ、VLにあつてはＶ−Ｊ構造を有する機
能的な遺伝子である。しかして、本発明において
ヒト以外の動物としてはマウス、ラツト、サル、
羊、ウサギ等であり、また、抗体産生細胞として
は好ましくはハイブリドーマ、クローン化Ｂ細胞
或はエプスタインバールウイルスによる計質転換
Ｂ細胞を用いることが望ましく、発現ベクターと
してはpSV2−gpt、pSV2−neo、SV40が好適で
ある。動物培養細胞には、ヒト、サル、マウス等
の動物に由来するリンパ腫を、腎細胞、Ｌ細胞、
COS細胞、HeLa細胞の何れかを用いることがで
きる。 しかして、本発明に従えばヒト以外の動物は自
由に免疫できるので容易に所望のキメラモノクロ
ーナル抗体を得ることができると共に、人間に投
与した場合動物由来のモノクローナル抗体に比し
て異種蛋白による抗原性が著しく軽減されること
が期待される。 次に実施例をもつて本発明を説明する。 実施例 マウスＶ遺伝子の単離 腫瘍細胞P3U1（アルバートアインシユタイン大
学のM.Scharff氏より供与された。Current
Topics in Microbiology and Immunology 81、
１−７、1978）とC57BL／６マウスに自然発生
した黒色腫瘍細胞で免疫したC57BL／６マウス
に由来する脾臓細胞との融合細胞であるハイブリ
ド−マD10株（注、D10株は、本願発明者の一人
である谷口克が確立したメラノーマ細胞に反応す
る抗体を産生する細胞であるM2590株のサブライ
ン（sub−line）で、正式にはM2590・D10株と
名付けられていた。ただ、Labノートから記載す
るにあたつてD10と呼称している。従つて、D10
株はM2590株に由来するものである。J.Invest.
Dermatol.83：128−133、1984）は黒色腫瘍細胞
と選択的に反応する抗体を分泌し、この抗体のタ
イプはＨ鎖についてはIgM型で、Ｌ鎖については
κである。先づD10株、P3U1株及びC57BL／６
マウス腎臓からDNAを単離す（Cell24353−356
（1981）参照）次に10μｇのDNAを制限酵素Hind
とEcoRで切断する。制限酵素のHindで切
断したD10株とP3U1株及びC57BL／６マウス腎
臓のDNAを電気泳動で0.9％のアガロースゲルに
展開し、ニトロセルロース膜（Schleicher and
Schvell、J.Mol.Biol.98503〜515（1975）参照）に
転写し、一方J〓領域を含んだ2.7Kb Hind−
Hind断片に相当する（利根川進氏より得た。
Nature280288〜294（1979）参照）J〓プローブ
（107cpm／0.1DNA）を用いたハイブリダゼーシ
ヨンを行つた。その結果を図１Aaに示す。 ところで図１Aaより明らかなようにD10株の
DNAは6.5、6.3及び6.1Kbの３つの再配列したバ
ンドが存在する。これらのうち6.3及び6.1Kbは
P3U1DNAに見られるものと同様のものである。
6.5KbのバンドはV〓−J〓構造を含む活性な遺伝子
であり、その特異性の発現に関与する遺伝子であ
る。分子サイズはλフアージのHindマーカー
によつて見積つた。このサイズに相当するDNA
断片をアガロース電気泳動により単離し、λフア
ージHindベクターλ788（K.Murray氏（エジン
バラ大学）より得た。Mole.Genet.15053−61
（1977）参照）に挿入し、λフアージにパツケー
ジした。パツケージミクスチヤーには大腸菌
BHB2688とBHB2690を用いた。（Hohn.B.Meth.
Enzymol68299−309（1979）参照）次にJ〓プロー
ブをスクリーニングに用いベントンデイビス法
（Science196180−182（1977）参照）にしたがつて
プラークハイブリダイゼーシヨンを行いクローン
VJ〓14を単離した。このクローンの制限酵素地図
を表Baに示す。このクローンVJ〓14のHind
挿入断片をノーザンハイブリダイゼーシヨンを行
うために単離した。 D10株からグアニジニウムチオシアネート法
（Biochemistry185294〜5299（1979）参照）によ
り全RNAを分離し、オリゴdTセルロースカラム
の巣通り画分からポリＡ構造をもつmRNAを得
た。図１AbはD10株のmRNAと、クローンVJ〓
14のHind挿入断片或はC〓領域を含む3KbHind
−BamH断片（利根川進氏より得た。
Nature280288−294（1979）参照）に相当するC〓
プローブとのノーザンハイブリダイゼーシヨンを
示している。J〓とC〓の両プローブにより1.2Kbの
位置にバンドが見つかつた。クローンVJ〓14は機
能的なV〓−J〓構造を含んでいる。 ノーザンハイブリダイゼーシヨンの方法は免疫
実験操作法Ｘ（1983）に記載されている。 また、図１Acは0.9KbのXba−EcoR断片
に相当するJHプローブ（Cell24353−365（1981）
参照）とEcoRで切断したDNAのサザンハイブ
リダイゼーシヨンを示す。先に述べた理由を基に
D10株DNAだけ探索される5.5KbのDNAを機能
的なＨ鎖のＶ領域遺伝子を含む断片λフアージ
EcoRベクターであるλgtWES−λB（P.Leader.
Science196175−177（1977）参照）を用いてクロ
ーン化し、クローンVJH243を得た。クローンVJH
243とMEP203（Proc.Natl.Acad.Sci.USA772138
−2142（1980）参照）の10KbのEcoR断片に相
当するCμプローブを用いた。D10株のmRNAと
ノーザンブロツテングを行つた結果、2.4Kbの位
置にバンドを見つけた（図１Ad参照）。クローン
VJ〓14とVJH243に含まれる活性なＶ遺伝子が特異
性の発現に関与する。 ヒトＣ遺伝子の単離 ヒトの血漿の中で主要な免疫グロブリンクラス
であるIgGの定常領域の遺伝子を単離する。すな
わちヒトの免疫グロブリン遺伝子の塩基配列はマ
ウスのそれと高い相同性を示しているので、ヒト
のゲノムに存在する例えばC〓とC〓１遺伝子をそれ
に相当するマウスの遺伝子をプローブとして用い
て単離するものであつて、その方法はクローン
Ig146（Proc.Natl.Acad.Sci.USA754709−4713
（1978）参照）からの3KbのHind−BamHI断
片とクローンMEP10（Proc.Natl.Acad.Sci.USA.
78474−478（1981）参照）からの6.8KbのEcoR
断片をプローブとして用いヒトのラムダ
charon4AのHae−Alu遺伝子ライブラリー
（T.Maniatis、Cell.151157−1174（1978）参照）
中からヒトC〓遺伝子を含みエンハンサー領域を保
持している断片を単離する。C〓１遺伝子はヒト胎
児肝細胞DNAをHindで切断しアガロースゲル
電気泳動で大きさにしたがつて分画したのち
5.9Kbのバンドをλ788に挿入し前記のプローブを
用いてクローン化した。単離したクローンは図１
BcのHC〓２とｄのHG163である。 V〓（マウス）遺伝子とC〓（ヒト）遺伝子を含むプ
ラスミドpSV2−HC〓VD10作成 エンハンサーを保持したヒトC〓遺伝子を含む
1.9KbのPvu断片を図１Bcに示すクローンHC〓
２から単離し等量混合したHindとBamH1リン
カー（宝酒造(株)製）を結合したのちHindで切
断する。この切断を図１Baに示すVJ〓14から単離
した6.5KbのHind挿入断片と結合し、BamH1
で切断する。得られた断片を分別しアガロースゲ
ル電気泳動により5.9Kbの断片を単離する。この
断片をpSV2gptのBamH1部位に挿入する。挿入
した遺伝子の方向は、制限地図により決定する。
（図２apSV2−HC〓VD10参照） VH（マウス遺伝子Cγl（ヒト）遺伝子を含むプラス
ミドpSV2−HG1VD10作成 8.2KbのHind挿入断片をHG163クローンか
ら単離し、Klenov酸素により両端の一本鎖部分
を消化し、その両端にEcoRリンカー（宝酒造
(株)製）を接続した。その断片をEcoRとBamH
で切断しEcoRとBamHIで閉環したプラスミ
ドpSV2gptに挿入し、ヒトCγ1遺伝子を含む
pSV2−HG14クローンを得る。5.5KbのEcoR
断片をクローンVJH243から単離しpSV2−HG14
のEcoR切断位置に挿入する。挿入した遺伝子
の方向は制限地図により決定した。（図２ｂ
pSV2−HGIVD10参照） プラスミドpSV2−HC〓VD10及びpSV2−HC1VD10
による形質細胞腫の形質転換 pSV2−HC〓VD10とpSV2−HG1VD10の両DNA
をカルシウム、リン酸共沈降法（proc.Natl、
Acad.Sci.USA76 1373−1376（1979参照）により
プラズマサイトーマ（形質細胞腫）P3U1株（Ｈ
鎖は合成しないがＬ鎖を生産する性質を持つ）に
導入した。その方法は次のとおりである。 １ Ａ溶液をそれと等量の2xHeBS溶液に滴下す
る。 ２ 室温で30分間保温する。 ３ P3U1株をトリプシン処理し、細胞をばらば
らにした後10％牛胎児血清を含むRPMI1640培
地を加えトリプシン処理を終了させる。 ４ 培養液を1500rpm5分間遠心して細胞を集め
る。 ５ 牛胎児血清を含まない培値に２×107個の細
胞を滴下する。 ６ 1500rpmで５分間遠心する。 ７ 直接、１の液10mlに浮遊する。 ８ 37℃で30分間保温する。 ９ ５mlの別の試験管に移す。 10 10％牛胎児血清を含むRPMI1640の培地をそ
れぞれ45mlずつ加える。 11 96穴プレートにそれぞれ0.1mlずつ２×104個
の細胞が入る様に分注する。 12 72時間RPMI1640−10％牛胎児血清培地で培
養する。 13 その後5μｇ／mlのミコフエノール酸と250μ
ｇ／mlのキサンチンを含むRPMI1640−10％牛
胎児血清培地にとりかえ、形質転換した細胞を
選択する。 しかして、Ａ溶液及び2xHeBS溶液は次のよう
な組成を有する。 【表】 キメラモノクローナル抗体産生形質転換細胞の選
別 キメラモノクローナル抗体産生形質転換細胞の
選別には酵素免疫〔−〕蛍光抗体法、或はセルソ
ーター（FACS）（ベクトン・デツキンソン社）
による解析を用いた。ミコフエノール酸を含む選
択培地により18の形質転換細胞クローンが選別さ
れた。それら選別された18の細胞に、それぞれ
HMH−S1からHMH−S18と名付けた。P3U1株
とこれら18の形質転換細胞はプレート中に十分増
殖するまで選別培地で育てた。これらの一部の細
胞の培養上清を酵素免疫蛍光抗体法（Meth.
Enzymol.70419−439（1980）参照）によつて抗体
の産生状態を試験した。その結果を表１に示す。 【表】 この内、HMH−S7は１×107個の細胞が10ml
の培養上清に約100nｇ／mlのマウス・ヒトキメ
ラモノクローナル抗体を産生している。 抗ヒトIgGを用いたHMH細胞とP3U1のセルソー
ター解析 HMH細胞とP3U1株はHank′sの平衡塩類溶液
（Gibco）で２度洗浄し107個の細胞を750μの染
色緩衝液（１％、FCS−RPMI1640）と250μの
ウサギ抗ヒト免疫グロブリン抗体又は正常ウサギ
IgG（1μｇ／ml）の混合液に浮遊させ、１時間室
温で保温した。その後細胞を３度洗浄した。その
後の手順はベクターラボラトリ社のアビジンビオ
チンキツト（avidine biotinekit）に示されてい
るものと同様である。要領としては細胞を予めヒ
トIgGで吸収処理したビオチン結合抗ウサギIgG
（1.5ｍｇ／ml）200倍希釈溶液250μに浮遊し、
１時間、室温で保温した後、Hank′s溶液で３度
洗浄し、250μの20倍希釈アビジンFITC（５ｍ
ｇ／ml）に浮遊させ室温で30分間保温し、
Hank′s溶液で３度洗浄する。最後に106個の細胞
を１mlの培養液に浮遊させ、対数増幅器付きの
FACS（ベクトン・デイクソン社）で解析し
た。その結果を図３に示す。図３ａ，ｂ，ｃは標
的細胞としてHMH細胞を用いウサギIgGの反応
をコントロールとし、それぞれａはウサギの抗ヒ
トIg抗体、ｂはウサギの抗ヒトκ抗体、ｃはウサ
ギの抗ヒトIgGFc抗体との反応を表わし、ｄ，
ｅ，ｆはHMH細胞とP3U1細胞に対するそれぞ
れｄはウサギの抗ヒトIg抗体、ｅはウサギの抗ヒ
トκ抗体、ｆはウサギの抗ヒトIgGFc抗体の反応
を表わす。 HMH細胞に導入されたDNAの解析 HMH細胞から前述の方法によりDNAとポリ
Ａ構造を含むRNAを単離するHMH細胞のDNA
と同様に単離したC57BL／６腎臓細胞とP3U1細
胞のDNAをBamHで切断しJ〓（マウス）プロー
ブ（表4A−(a)）、C〓（ヒト）プローブ（表4A−
(b)）、JH（マウス）プローブ（表4A−(c)）及びC〓
（ヒト）プローブ（表4A−(d)）を用いサザンハイ
ブリダイゼーシヨンを行う。 ヒトC〓とマウスJ〓プローブはpSV2−HC〓VD10
のBamH挿入断片のサイズに相当する5.9Kbの
バンドをHMH細胞のDNA中に探索した。マウ
スJHプローブはpSV2−HGIVD10のVH遺伝子を含
むEcoR挿入断片に相当する5.5Kbのバンドを
HMH細胞のDNA中に探索した。ヒトC〓１プロ
ーブはpSV2−HG1VD10のC〓１遺伝子を含む
EcoR−RamH挿入断片をHMH細胞のDNA
中に探索した。これらによりHMH細胞にはゲノ
ム中に完全なＨ鎖とＬ鎖のキメラ遺伝子を保持し
ていることが示された。 HMH細胞より単離したポリＡ構造をもつｍ−
RNAとP3U1より単離したポリＡ構造をもつ
mRNAをそれぞれVJ〓14プローブ、ヒトC〓プロー
ブ、VJH243プローブ及びヒトC〓１プローブとの
間でノーザンブロツテングを行つた。VJ〓14プロ
ーブとヒトC〓プローブにより通常Ｋ鎖を生産して
いる細胞にみられるのと同じサイズに相当する
1.2Kbのバンドがキメラ抗体のＬ鎖のmRNAとし
て探索され、HMH細胞のmRNA中に最初に転
写されたもので、またスプライジングされていな
いためイントロンがとり除かれていないmRNA
が5Kbのバンドとして探索される。（図４Ba，ｂ
参照）VJH243としてC〓１プローブによりHMH細
胞のmRNM中に3.5Kbと7Kbのバンドが探索さ
れ、3.5Kbのバンドは膜結合型のγH鎖のmRNA
のサイズに相当し、7Kbのバンドは最初に転写さ
れイントロンがとり除かれていないmRNAに相
当する。 以上によりHMH細胞中でマウス由来のＶ−(D)
−Ｊエクソンとヒト由来のＣエクソンの間で最初
に転写されたmRNAのスプライシングが部分的
に起つていることが証明された。
【図面の簡単な説明】
図１Ａは活性なマウスＶ遺伝子とヒトのＣ遺伝
子を単離するためのサザンハイブリダイゼーシヨ
ン及びそれらのmRNAのノーザンブロツテング
の解析結果を示すＸ線写真、Ｂは単離したクロー
ンの制限酵素地図、 図中Eoはエンハンサー、ＨはHind、Ｂは
BamH、ＥはEcoR、ＰはPvuを表わす、 図２はDNA形質転換に用いるために作成した
プラスミド構造、 ａ……プラスミドpSV2−HC〓VD10の構造、ｂ
……プラスミドpSV2−HGIVD10の構造、 図３はセルソーター解析図、図４ＡはHMH細
胞のDNAのサザンハイブリダイゼーシヨン、Ｂ
はHMH細胞のmRNAのノーザンブロツテング
解析結果を示すＸ線写真。

Claims (1)

  1. 【特許請求の範囲】 １ ヒト以外の動物の抗体産生細胞のDNAから
    単離した活性なVHとVL遺伝子、及び、ヒトDNA
    から単離したCHとCL遺伝子を、VLの下流にCLを、
    VHの下流にCHをそれぞれ配列して発現ベクター
    に挿入し、該発現ベクターを動物培養細胞に導入
    してキメラモノクロナール抗体を産生することを
    特徴とするヒト以外の動物由来の可変領域とヒト
    由来の定常領域とからなるキメラモノクロナール
    抗体の製造方法。 ２ 抗体生産細胞としてハイブリドーマ、エプス
    タインバールヴイルスによる形質転換Ｂ細胞また
    はクローン化Ｂ細胞を用いる特許請求の範囲第１
    項記載のキメラモノクロナール抗体の製造方法。 ３ ベクターとしてpSV2−gpt、pSV2−neo、
    SV40からなる群から選ばれたベクターを使用す
    ることからなる特許請求の範囲第１項記載のキメ
    ラモノクロナール抗体の製造方法。 ４ 動物培養細胞がヒト、サル、マウス等の動物
    に由来するリンパ腫、腎細胞、Ｌ細胞、COS細
    胞、HeLa細胞の何れか一種を使用する特許請求
    の範囲第１項記載のキメラモノクロナール抗体の
    製造方法。
JP16937084A 1984-08-15 1984-08-15 キメラモノクロ−ナル抗体及びその製造法 Granted JPS6147500A (ja)

Priority Applications (5)

Application Number Priority Date Filing Date Title
JP16937084A JPS6147500A (ja) 1984-08-15 1984-08-15 キメラモノクロ−ナル抗体及びその製造法
DE19853587360 DE3587360T2 (de) 1984-08-15 1985-03-08 Verfahren zur Herstellung von chimärischen monoklonalen Antikörpern.
DE1985102665 DE171496T1 (de) 1984-08-15 1985-03-08 Chimaerischer monoklonaler antikoerper und verfahren zu seiner herstellung.
EP85102665A EP0171496B1 (en) 1984-08-15 1985-03-08 Process for the production of a chimera monoclonal antibody
CA 476731 CA1339201C (en) 1984-08-15 1985-03-18 Chimera monoclonal antibody and a production process thereof

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP16937084A JPS6147500A (ja) 1984-08-15 1984-08-15 キメラモノクロ−ナル抗体及びその製造法

Publications (2)

Publication Number Publication Date
JPS6147500A JPS6147500A (ja) 1986-03-07
JPH0373280B2 true JPH0373280B2 (ja) 1991-11-21

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ID=15885326

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EP (1) EP0171496B1 (ja)
JP (1) JPS6147500A (ja)
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DE (2) DE3587360T2 (ja)

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WO2015033831A1 (ja) 2013-09-04 2015-03-12 国立大学法人 大阪大学 Ｄｐｐ－４を標的とした糖尿病治療用ワクチン
WO2015099167A1 (ja) 2013-12-27 2015-07-02 国立大学法人大阪大学 Ｉｌ－１７ａを標的とするワクチン
WO2020162452A1 (ja) 2019-02-04 2020-08-13 国立大学法人愛媛大学 ＣＡＲライブラリおよびｓｃＦｖの製造方法
WO2022014703A1 (ja) 2020-07-17 2022-01-20 田辺三菱製薬株式会社 筋疾患の予防または治療剤

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CA1339201C (en) 1997-08-05
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EP0171496B1 (en) 1993-05-26

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