JP2006170857A - 固体支持体上の生体分子を質量分析する方法およびそのための固体支持体 - Google Patents
固体支持体上の生体分子を質量分析する方法およびそのための固体支持体 Download PDFInfo
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Abstract
【解決手段】 生体分子を分析する方法であって、試料中の生体分子を固体支持体上に固定化すること、固体支持体上の生体分子を酵素で分解すること、および得られた分解物を質量分析することを含む前記方法。
【選択図】 図1
Description
(1)生体分子を分析する方法であって、
試料中の生体分子を固体支持体上に固定化すること、固体支持体上の生体分子を酵素で分解すること、および得られた分解物を質量分析することを含む前記方法。
(2)試料中の生体分子をゲル電気泳動で分離し、ゲル中に分離された生体分子を固体支持体上に転写することにより、試料中の生体分子を固体支持体上に固定化する(1)記載の方法。
(4)固体支持体が表面にカーボン層を有するものである(1)〜(3)のいずれかに記載の方法。
(6)カーボン層が化学修飾されているものである(4)または(5)記載の方法。
(7)固体支持体上の生体分子にさらなる生体分子を相互作用させることをさらに含み、固体支持体上の生体分子および/または相互作用した生体分子を酵素で分解すること、ならびに得られた分解物を質量分析することを含む(1)〜(6)のいずれかに記載の方法。
(9)質量分析を、レーザ脱離/イオン化−飛行時間型質量分析によって行う(1)〜(8)のいずれかに記載の方法。
(10)(1)〜(9)のいずれかに記載の方法において使用するための表面にカーボン層を有する固体支持体。
(11)(1)〜(9)のいずれかに記載の方法において使用するためのキットであって、表面にカーボン層を有する固体支持体および酵素を含む前記キット。
静電層の厚みは、1nm〜500μmであることが好ましい。
固体支持体の作成
76mm×26mm×1.1mmのスライドガラスにTi層およびその上にPt層をマグネトロンスパッタリングにより形成した。スパッタリングの条件は以下の通りである。生成した金属層の厚みは、Ti層およびPt層それぞれが100nmであった。
Cy3-プロテインA(1.5μg、SIGMA社製)、大腸菌タンパク質(0.5μg)およびマーカー(Prestained Broad Range、0.5μl、BIO RAD社製)を試料として用い、SDS−PAGE用装置(ATTO社製 AE−7300型)を用いて電気泳動を行った。泳動用のゲルとしては、10%ポリアクリルアミドゲルを使用した。泳動用バッファーは0.1%SDSを含むグリシン―トリスバッファー(pH8.3)を用い、泳動は200Vで35分間行った。泳動終了後、15分間CBB染色し、脱染色したあと、LAS1000(富士写真フイルム株式会社製)で画像撮影した(図1)。約50kDa付近にCy3-プロテインAのバンドが検出された。
泳動後のポリアクリルアミドゲルを、あらかじめ冷却しておいた転写用バッファー(25mM Tris、5%メタノール)に30分間浸漬し、平衡化した。次いで、ポリアクリルアミドゲルを固体支持体1に載る大きさに切り取って、該固体支持体と密着させ、ポリアクリルアミドゲルを陰極、固体支持体を陽極に設置し、下記条件で通電した。
タンパク質転写後の固体支持体1の蛍光強度をFLA8000(富士写真フイルム株式会社製)で測定したところ、蛍光強度が28270として測定され、Cy3−プロテインAが固体支持体表面に固定化されたことが確認された(図2)。続いて、該固体支持体をPBSで10分間洗浄した後、同様に蛍光強度を測定したところ、蛍光強度は9766であり、約1/3程度まで低下した(図3)。ブロッキング試薬(Roche社製)で1時間ブロッキングし、蛍光強度を測定したところ蛍光強度に変化はなかった。次ぎに、500μlの0.05μg/μl Cy3−IgGを添加して室温で1時間反応させた後、PBSで室温にて12時間洗浄し、蛍光強度を測定した(図4)。蛍光強度は16448であり、増加していることから、プロテインAとIgGが結合したこと、すなわち、転写保持されたタンパク質の結合能が維持されたことがわかる。
ステンレス−DLC固体支持体の作成
ステンレス基板にダイヤモンドライクカーボン層を形成した。ステンレス基板は、平滑性と蛍光バックグラウンドを下げるために、予めバフ研磨後、更に電解研磨を施した。ダイヤモンドライクカーボン層の形成はイオン化蒸着法により以下の条件で行った。生成したダイヤモンドライクカーボン層の厚みは、20nmであった。また、アンモニアプラズマ処理することによりアミノ基を導入することにより固体支持体2を作成した。
Cy3−プロテインA(50ng、SIGMA社製)およびCy3−IgA(100ng、SIGMA社製)を実施例1と同様にSDS−PAGE法(ATTO社製 AE−6530型)で泳動し、泳動終了後、15分間CBB染色し、脱染色したあと、LAS1000(富士写真フイルム株式会社製)で画像撮影した(図8)。なお、Cy3-IgAの泳動については、12%ポリアクリルアミドゲルを使用した。また、実施例2と同様にして、固体支持体2を作成した。
実施例1と同様にして基板1にダイヤモンドライクカーボン層を形成し、イオン化蒸着装置を用いてアンモニアプラズマ中で処理することにより表面をアミノ化して固体支持体3を作成した。
Cy3ラベルした酵母タンパク質(300μg/レーン)を実施例1と同様にSDS−PAGE法(ATTO社製 AE−6530型)で泳動し、泳動終了後、FLA8000(富士写真フイルム株式会社製)で画像撮影した(図14(1))。また、実施例2と同様にして、固体支持体2を作成した。
その結果、転写効率が約40%であり、十分転写ができていることが判明した。
Cy3−プロテインA(50ng、SIGMA社製)とCy5−IgA(100ng、SIGMA社製)を溶液中で混合し、Native−PAGE法(ATTO社製 AE−6530型)で泳動し、泳動終了後、FLA8000(富士写真フイルム株式会社製)で画像撮影した。また、実施例2と同様にして、固体支持体2を作成した。
(1)固体支持体上でタンパク質をトリプシン消化した場合
牛アルブミン(BSA)を実施例2で作製した固体支持体2にスポットした。スポットしたBSAにトリプシン消化液(100mM NH4HCO3、0.3μg/μl トリプシン)をのせて37℃で16時間にわたり酵素消化した。マトリックス溶媒(1mg/mL α-シアノヒドロキシ桂皮酸、50%アセトニトリル、0.1%トリフルオロ酢酸)をスポットし、自然乾燥後、MALDI−TOF MS測定した。
(2)溶液中でタンパク質をトリプシン消化した場合
牛アルブミン(BSA)をトリプシン消化液中で、37℃にて5時間にわたり酵素消化した。消化後のBSAを固体支持体2にスポットし、さらに自然乾燥後、MALDI−TOF MS測定した。
(3)トリプシン消化なしの場合
牛アルブミン(BSA)を実施例2で作製した固体支持体2にスポットした。スポットしたBSAに(1)と同じマトリックス溶媒をスポットし、自然乾燥後、MALDI−TOF MS測定した。
酵母(Saccharomyces cerevisiae)から既知の方法によりタンパク質を抽出し、抽出物に対し、二次元電気泳動を行った。電気泳動にて分離させたタンパク質をゲルから実施例2で作製した固体支持体2に、実施例3と同様の方法において転写用バッファーC1を用いてブロッティング(転写)し、リジルエンドペプチダーゼ消化液(5mM Tris−HCl、pH9.0、1ug/mL リジルエンドペプチダーゼ)をのせて37℃で5時間にわたり酵素消化した。マトリックス溶媒(1mg/mL α-シアノヒドロキシ桂皮酸、50%アセトニトリル、0.1% TFA)をスポットし、自然乾燥後、MALDI−TOF MS測定した。それぞれのエリアから得られた質量スペクトルを用い、Mascotにてデータベースサーチを行ったところ、酵母由来のタンパク質であるフコース−ビスホスフェートアルドラーゼ(分子量:39465)、エノラーゼ 2(分子量:46754)およびチトクロム B pre−mRNA プロセシングプロテイン 2(分子量73814)と十分に高い相同性が得られ、これらのタンパク質を同定することができた。
Claims (11)
- 生体分子を分析する方法であって、
試料中の生体分子を固体支持体上に固定化すること、固体支持体上の生体分子を酵素で分解すること、および得られた分解物を質量分析することを含む前記方法。 - 試料中の生体分子をゲル電気泳動で分離し、ゲル中に分離された生体分子を固体支持体上に転写することにより、試料中の生体分子を固体支持体上に固定化する請求項1記載の方法。
- 試料中の生体分子をゲル電気泳動で分離し、ゲル中に分離された生体分子をメンブレン上に転写し、該メンブレン上に転写された生体分子を固体支持体上に転写することにより、試料中の生体分子を固体支持体上に固定化する請求項1記載の方法。
- 固体支持体が表面にカーボン層を有するものである請求項1〜3のいずれか1項記載の方法。
- カーボン層が、ダイヤモンドライクカーボン層である請求項4記載の方法。
- カーボン層が化学修飾されているものである請求項4または5記載の方法。
- 固体支持体上の生体分子にさらなる生体分子を相互作用させることをさらに含み、固体支持体上の生体分子および/または相互作用した生体分子を酵素で分解すること、ならびに得られた分解物を質量分析することを含む請求項1〜6のいずれか1項記載の方法。
- 生体分子がペプチドであり、酵素がプロテアーゼである請求項1〜7のいずれか1項記載の方法。
- 質量分析を、レーザ脱離/イオン化−飛行時間型質量分析によって行う請求項1〜8のいずれか1項記載の方法。
- 請求項1〜9のいずれか1項記載の方法において使用するための表面にカーボン層を有する固体支持体。
- 請求項1〜9のいずれか1項記載の方法において使用するためのキットであって、表面にカーボン層を有する固体支持体および酵素を含む前記キット。
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