JPH0446200A - Protein immobilizing material - Google Patents
Protein immobilizing materialInfo
- Publication number
- JPH0446200A JPH0446200A JP15360090A JP15360090A JPH0446200A JP H0446200 A JPH0446200 A JP H0446200A JP 15360090 A JP15360090 A JP 15360090A JP 15360090 A JP15360090 A JP 15360090A JP H0446200 A JPH0446200 A JP H0446200A
- Authority
- JP
- Japan
- Prior art keywords
- copolymer
- vinyl monomer
- active ester
- ester group
- protein
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 20
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 20
- 239000000463 material Substances 0.000 title claims abstract description 15
- 230000003100 immobilizing effect Effects 0.000 title abstract 3
- 229920001577 copolymer Polymers 0.000 claims abstract description 23
- 239000000178 monomer Substances 0.000 claims abstract description 18
- 125000000391 vinyl group Chemical group [H]C([*])=C([H])[H] 0.000 claims abstract description 16
- 229920002554 vinyl polymer Polymers 0.000 claims abstract description 16
- 125000004185 ester group Chemical group 0.000 claims abstract description 10
- 230000002209 hydrophobic effect Effects 0.000 claims abstract description 7
- PPBRXRYQALVLMV-UHFFFAOYSA-N Styrene Chemical compound C=CC1=CC=CC=C1 PPBRXRYQALVLMV-UHFFFAOYSA-N 0.000 abstract description 9
- 239000002861 polymer material Substances 0.000 abstract description 5
- KAKZBPTYRLMSJV-UHFFFAOYSA-N Butadiene Chemical compound C=CC=C KAKZBPTYRLMSJV-UHFFFAOYSA-N 0.000 abstract description 4
- 150000002148 esters Chemical class 0.000 abstract description 4
- VVQNEPGJFQJSBK-UHFFFAOYSA-N Methyl methacrylate Chemical compound COC(=O)C(C)=C VVQNEPGJFQJSBK-UHFFFAOYSA-N 0.000 abstract description 3
- 238000006243 chemical reaction Methods 0.000 abstract description 3
- IRQWEODKXLDORP-UHFFFAOYSA-N 4-ethenylbenzoic acid Chemical compound OC(=O)C1=CC=C(C=C)C=C1 IRQWEODKXLDORP-UHFFFAOYSA-N 0.000 abstract description 2
- CERQOIWHTDAKMF-UHFFFAOYSA-N Methacrylic acid Chemical compound CC(=C)C(O)=O CERQOIWHTDAKMF-UHFFFAOYSA-N 0.000 abstract description 2
- BZHJMEDXRYGGRV-UHFFFAOYSA-N Vinyl chloride Chemical compound ClC=C BZHJMEDXRYGGRV-UHFFFAOYSA-N 0.000 abstract description 2
- 238000000807 solvent casting Methods 0.000 abstract description 2
- WYURNTSHIVDZCO-UHFFFAOYSA-N Tetrahydrofuran Chemical compound C1CCOC1 WYURNTSHIVDZCO-UHFFFAOYSA-N 0.000 description 10
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 8
- 239000010408 film Substances 0.000 description 7
- 239000012528 membrane Substances 0.000 description 7
- 238000006116 polymerization reaction Methods 0.000 description 7
- KZNICNPSHKQLFF-UHFFFAOYSA-N succinimide Chemical compound O=C1CCC(=O)N1 KZNICNPSHKQLFF-UHFFFAOYSA-N 0.000 description 6
- YLQBMQCUIZJEEH-UHFFFAOYSA-N tetrahydrofuran Natural products C=1C=COC=1 YLQBMQCUIZJEEH-UHFFFAOYSA-N 0.000 description 5
- 102000009027 Albumins Human genes 0.000 description 4
- 108010088751 Albumins Proteins 0.000 description 4
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 4
- -1 nitrophenol ester Chemical class 0.000 description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 4
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- YXFVVABEGXRONW-UHFFFAOYSA-N Toluene Chemical compound CC1=CC=CC=C1 YXFVVABEGXRONW-UHFFFAOYSA-N 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 229960002317 succinimide Drugs 0.000 description 3
- UFHSKEHEWFGEFH-UHFFFAOYSA-N (2,5-dioxopyrrolidin-3-yl) prop-2-enoate Chemical compound C=CC(=O)OC1CC(=O)NC1=O UFHSKEHEWFGEFH-UHFFFAOYSA-N 0.000 description 2
- 229920002799 BoPET Polymers 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 102000016359 Fibronectins Human genes 0.000 description 2
- 108010067306 Fibronectins Proteins 0.000 description 2
- 239000000560 biocompatible material Substances 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 125000006575 electron-withdrawing group Chemical group 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 229910052757 nitrogen Inorganic materials 0.000 description 2
- 229920000139 polyethylene terephthalate Polymers 0.000 description 2
- 239000005020 polyethylene terephthalate Substances 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000010409 thin film Substances 0.000 description 2
- SMZOUWXMTYCWNB-UHFFFAOYSA-N 2-(2-methoxy-5-methylphenyl)ethanamine Chemical compound COC1=CC=C(C)C=C1CCN SMZOUWXMTYCWNB-UHFFFAOYSA-N 0.000 description 1
- NIXOWILDQLNWCW-UHFFFAOYSA-N 2-Propenoic acid Natural products OC(=O)C=C NIXOWILDQLNWCW-UHFFFAOYSA-N 0.000 description 1
- YLZOPXRUQYQQID-UHFFFAOYSA-N 3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)-1-[4-[2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidin-5-yl]piperazin-1-yl]propan-1-one Chemical compound N1N=NC=2CN(CCC=21)CCC(=O)N1CCN(CC1)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F YLZOPXRUQYQQID-UHFFFAOYSA-N 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- 150000007945 N-acyl ureas Chemical class 0.000 description 1
- 239000004698 Polyethylene Substances 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 238000004833 X-ray photoelectron spectroscopy Methods 0.000 description 1
- 238000012644 addition polymerization Methods 0.000 description 1
- 239000000853 adhesive Substances 0.000 description 1
- 230000001070 adhesive effect Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 238000005266 casting Methods 0.000 description 1
- 230000021164 cell adhesion Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 239000004020 conductor Substances 0.000 description 1
- 238000007334 copolymerization reaction Methods 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000000034 method Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 125000004433 nitrogen atom Chemical group N* 0.000 description 1
- NMHMNPHRMNGLLB-UHFFFAOYSA-N phloretic acid Chemical compound OC(=O)CCC1=CC=C(O)C=C1 NMHMNPHRMNGLLB-UHFFFAOYSA-N 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 230000000379 polymerizing effect Effects 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000004814 polyurethane Substances 0.000 description 1
- 229920003225 polyurethane elastomer Polymers 0.000 description 1
- 229920000915 polyvinyl chloride Polymers 0.000 description 1
- 239000004800 polyvinyl chloride Substances 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- 229920002379 silicone rubber Polymers 0.000 description 1
- 239000004945 silicone rubber Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 238000005211 surface analysis Methods 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Landscapes
- Peptides Or Proteins (AREA)
- Addition Polymer Or Copolymer, Post-Treatments, Or Chemical Modifications (AREA)
Abstract
Description
【発明の詳細な説明】
（産業上の利用分野）
本発明は、活性エステル基を有するビニルモノマーと疎
水性ビニルモノマーとの共重合体による蛋白質固定化材
料に関する。DETAILED DESCRIPTION OF THE INVENTION (Field of Industrial Application) The present invention relates to a protein immobilization material made of a copolymer of a vinyl monomer having an active ester group and a hydrophobic vinyl monomer.
（従来の技術・発明が解決しようとする課Ｂ）現在まで
に５種々の蛋白質を表面に導入した生体適合性材料が知
られているが、高分子材料表面を改質し細胞接着性又は
非接着性表面を得る方法として前者はフィブロネクチン
、コラーゲン等の細胞接着性蛋白質を、後者はアルブミ
ン等の蛋白質を高分子材料表面に塗布、吸着させること
により得られる。しかし、これらの生体適合性材料は高
分子材料の材質により表面への蛋白質の吸着しやすさに
差があり、また表面に蛋白質を塗布吸着させた場合２体
液や血液と接触すると経時的に吸着蛋白質の脱離および
他の蛋白質との交換が起こる等の問題点を有していた。(Problem B to be solved by the conventional technology/invention) Until now, five types of biocompatible materials have been known that have various proteins introduced onto their surfaces. The adhesive surface can be obtained by coating and adsorbing cell adhesion proteins such as fibronectin and collagen on the surface of a polymeric material in the former and by adsorbing proteins such as albumin in the latter. However, these biocompatible materials differ in the ease with which proteins can be adsorbed to the surface depending on the polymer material, and when proteins are coated on the surface and adsorbed, the adsorption may occur over time when it comes into contact with body fluids or blood. This method had problems such as protein desorption and exchange with other proteins.
そこで９本発明は、蛋白質を確実に吸着・固定化するこ
とができ、しかも任意の蛍白質を吸着・固定化すること
ができる蛋白質固定化材料を提供することを課題とする
。Therefore, an object of the present invention is to provide a protein immobilization material that can reliably adsorb and immobilize proteins, and can also adsorb and immobilize arbitrary fluorescent substances.
（課題を解決するための手段）
本発明者らは、かかる現況にかんがみ、活性エステル基
を有するビニルモノマーと疎水性子ツマ−との共重合に
よる蛋白質固定化材料を鋭意研究した結果１本発明に到
達したものである。(Means for Solving the Problems) In view of the current situation, the present inventors have conducted intensive research on protein immobilization materials made by copolymerizing a vinyl monomer having an active ester group and a hydrophobic monomer, and as a result have achieved the present invention. It has been reached.
すなわち１本発明は、活性エステル基を有するビニルモ
ノマーと疎水性ビニルモノマーとの共重合体からなるこ
とを特徴とする蛋白質固定化材料を要旨とする。That is, one aspect of the present invention is a protein immobilization material characterized by being composed of a copolymer of a vinyl monomer having an active ester group and a hydrophobic vinyl monomer.
以下２本発明の詳細な説明する。Two aspects of the present invention will be described in detail below.
本発明における活性エステル基を有するビニルモノマー
としては１例えばアクリル酸、メタクリル酸、４−ビニ
ル安思香酸等の電子吸引性基を持つエステル誘導体であ
ることが好ましい。このような電子吸引性基のエステル
としてはＮ−ヒドロキシコハク酸イミドエステル、ニト
ロフェノールエステル、クロロフェノールエステル、イ
ミタソールエステル等があげられる。また、カルボキン
ルア４ ヲ持つビニルモノマーのカルボンミニ水ｈｘ導
体、○〜アシル尿素誘導体等であってもよい。The vinyl monomer having an active ester group in the present invention is preferably an ester derivative having an electron-withdrawing group, such as acrylic acid, methacrylic acid, or 4-vinyl benzoic acid. Examples of such esters having an electron-withdrawing group include N-hydroxysuccinimide ester, nitrophenol ester, chlorophenol ester, and imitasol ester. Further, a carboxone mini water hx conductor of a vinyl monomer having carboquinure 4, a ~acylurea derivative, etc. may be used.
本発明における疎水性モノマーとしてはスチレン、メチ
ルメタクリレート１塩化ビニル、ブタジェン等があげら
れる。Examples of the hydrophobic monomer in the present invention include styrene, methyl methacrylate, vinyl monochloride, and butadiene.
本発明における共重合体の合成条件は一般の付加重合に
よる合成法と同様である。例えば、溶媒としては、使用
するビニルモノマーが？容解すればいかなるものでもよ
いが９例えばテトラヒドロフラン１ ヘンゼン、トルエ
ン、クロロホルムなどがあげられる。反応温度は任意で
よいが、０〜１００゛Ｃが好適である。また反応時間も
任意でよいが。The conditions for synthesizing the copolymer in the present invention are the same as those for general addition polymerization. For example, what kind of vinyl monomer should be used as a solvent? Any material may be used as long as it dissolves, but examples include tetrahydrofuran, toluene, and chloroform. The reaction temperature may be arbitrary, but 0 to 100°C is suitable. Also, the reaction time may be arbitrary.
１分〜２４時間が好適である。共重合組成比は任意でよ
いが、活性エステル基を有するビニルモノマーの割合が
０．１〜９０ｍｏ１％であることが好ましい。1 minute to 24 hours is suitable. Although the copolymerization composition ratio may be arbitrary, it is preferable that the proportion of the vinyl monomer having an active ester group is 0.1 to 90 mo1%.
本発明における共重合体は、単体で使用可能であるが、
用途に応じて溶媒キャストにより各種の高分子材料表面
に造膜してもよい。このような高分子材料としてはいか
なる高分子でもよく１例えばポリエステル、ポリウレタ
ン、シリコーンゴム。The copolymer in the present invention can be used alone, but
Films may be formed on the surfaces of various polymeric materials by solvent casting depending on the application. Such polymeric materials may be any polymers, such as polyester, polyurethane, and silicone rubber.
ポリ塩化ビニル、ポリスチレン、ポリエチレンシリカゲ
ル、でんぷん等があげられる。Examples include polyvinyl chloride, polystyrene, polyethylene silica gel, and starch.
本発明における共重合体をキャストした高分子材料は任
意の蛋白質を活性エステル基との化学反応により固定化
が可能である。The polymer material in which the copolymer of the present invention is cast can immobilize any protein through a chemical reaction with an active ester group.
（実施例） 次に１本発明を実施例により具体的に説明する。(Example) Next, one embodiment of the present invention will be specifically explained using examples.
実施例１
重合管にアクリロキシスクシンイミド６００ｍｇ、スチ
レンモノマー１４００ｍｇを加え、テトラヒドロフラン
１．０ ｍ １．を加えて溶解させ１更に濃度６．６ｍ
ｇ７ｍｆ２のアブビスイソブチロニトリルのテトラヒド
ロフランン容液を１． Ｏｍ １．加え７重合管を液体
窒素で冷却し減圧下で封管した。Example 1 600 mg of acryloxysuccinimide and 1400 mg of styrene monomer were added to a polymerization tube, and 1.0 m of tetrahydrofuran was added. Add and dissolve 1 to a further concentration of 6.6 m
A solution of 7 mf2 of abbisisobutyronitrile in tetrahydrofuran was added to 1. Om 1. In addition, the polymerization tube was cooled with liquid nitrogen and sealed under reduced pressure.
この重合管を６０″Ｃインキユベーターに入れて３時間
重合後、共重合体溶液をエチルエーテルに加えて共重合
体を析出させ、共重合体を遠心沈降により回収した。減
圧乾燥後、６００ｍｇのスクシンイミドを含有する共重
合体を得た。This polymerization tube was placed in a 60"C incubator and after polymerization for 3 hours, the copolymer solution was added to ethyl ether to precipitate the copolymer, and the copolymer was recovered by centrifugal sedimentation. After drying under reduced pressure, 600 mg A copolymer containing succinimide was obtained.
参考例１
実施例１で合成した共重合体５ｍｇをクロロホルム５０
０μｌに溶解し、ポリエチレンテレフタレート（ＰＥＴ
）フィルム（２５Ｘ５０ｍｍ）上にキャストして製膜し
た。このキャストフィルムを０．１％アルブミン溶液に
４時間浸漬し、ＩＭＮａｃＩ！および純水で洗浄し、ア
ルブミン固定化膜を作製した。Reference Example 1 5 mg of the copolymer synthesized in Example 1 was added to 50 mg of chloroform.
Dissolve polyethylene terephthalate (PET) in 0 μl.
) A film was formed by casting on a film (25 x 50 mm). This cast film was immersed in a 0.1% albumin solution for 4 hours, and IMNacI! and washed with pure water to prepare an albumin-immobilized membrane.
比較のために、市販のスチレンポリマー（ｎ−１６００
〜１８００）５ｍｇをクロロホルム５００μｌに溶解し
、ＰＥＴフィルム上にキャストして製膜した。このキャ
ストフィルムを０．１％アルブミン溶液に４時間浸漬し
、ＩＭＮａＣｆｆおよび純水で洗浄し、アルブミン吸着
膜を作製した。For comparison, a commercially available styrene polymer (n-1600
~1800) was dissolved in 500 μl of chloroform and cast onto a PET film to form a film. This cast film was immersed in a 0.1% albumin solution for 4 hours and washed with IMNaCff and pure water to produce an albumin adsorption membrane.
作製した膜をＸ線光電子解析装置（ＥＳＣＡ）により表
面分析を行ったところ、スクシンイミドを含有する共重
合体を用いたアルブミン固定化膜がスチレン重合体のア
ルブミン吸着膜よりもＮ原子のピーク面積が約６倍量大
きがった。Surface analysis of the prepared membrane using an X-ray photoelectron analyzer (ESCA) revealed that the albumin-immobilized membrane using a copolymer containing succinimide had a higher N atom peak area than the albumin-adsorbed membrane made of styrene polymer. Approximately 6 times larger.
参考例２
実施例１で合成した共重合体２ ｍ、 ｇをクロロホル
ム２００μｐにン容解しＰＥＴフィルム（２５Ｘ５０ｍ
ｍ）にキャストとして製膜した。１ｍｇ／４ｍＩ！、の
この膜をフィブロネクチンに４時間浸漬し、ＩＭＮａＣ
ｎおよび純水で洗浄し フィブロネクチン固定化膜を作
製した。Reference Example 2 2 m, g of the copolymer synthesized in Example 1 was dissolved in 200 μp of chloroform, and a PET film (25×50 m
m) was cast into a film. 1mg/4mI! , the membrane was immersed in fibronectin for 4 hours, and IMNaC
A fibronectin-immobilized membrane was prepared by washing with n and pure water.
実施例２
重合管にアクリロキシスクシンイミド６００ｍｇ、メチ
ルメタクリレ−）−１４００ｍｇを加え。Example 2 600 mg of acryloxysuccinimide and 1400 mg of methyl methacrylate were added to a polymerization tube.
テトラヒドロフラン１． Ｑ ｍ Ｉ２を加えて溶解さ
せ更に濃度６．６ｍｇ／ｍｌのアブビスイソブチロニト
リルのテトラヒドロフラン溶液を１．０ ｍ ｌ加え重
合管を液体窒素で冷却し減圧下で封管した。Tetrahydrofuran 1. Q m I2 was added and dissolved, and 1.0 ml of a tetrahydrofuran solution of abbisisobutyronitrile having a concentration of 6.6 mg/ml was added, and the polymerization tube was cooled with liquid nitrogen and sealed under reduced pressure.
この重合管を６０℃で３時間重合後、共重合体溶液をメ
タノールに加えて共重合体を析出させ。After polymerizing this polymerization tube at 60° C. for 3 hours, the copolymer solution was added to methanol to precipitate the copolymer.
共重合体を遠心沈陣により回収した。減圧乾燥後。The copolymer was recovered by centrifugation. After drying under reduced pressure.
９５０ｍｇのスクシンイミドを含有する共重合体を得た
。A copolymer containing 950 mg of succinimide was obtained.
（発明の効果ン
本発明の蛋白質固定化材料によると、任意の蛍白質を簡
便かつ確実にその表面に固定化することができる。また
５本発明における共重合体は微量でも蛋白質を固定化で
きるので、薄膜にすることができ、薄膜の基材となる高
分子材料の持つ力学的特性を損なうことがない。(Effects of the Invention) According to the protein immobilization material of the present invention, any fluorescent substance can be immobilized on the surface easily and reliably.Furthermore, the copolymer of the present invention can immobilize proteins even in trace amounts. Therefore, it can be made into a thin film without impairing the mechanical properties of the polymer material that is the base material of the thin film.
Claims (1)
ビニルモノマーとの共重合体からなることを特徴とする
蛋白質固定化材料。(1) A protein immobilization material comprising a copolymer of a vinyl monomer having an active ester group and a hydrophobic vinyl monomer.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP15360090A JPH0446200A (en) | 1990-06-11 | 1990-06-11 | Protein immobilizing material |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP15360090A JPH0446200A (en) | 1990-06-11 | 1990-06-11 | Protein immobilizing material |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH0446200A true JPH0446200A (en) | 1992-02-17 |
Family
ID=15566030
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP15360090A Pending JPH0446200A (en) | 1990-06-11 | 1990-06-11 | Protein immobilizing material |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0446200A (en) |
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008530204A (en) * | 2005-02-21 | 2008-08-07 | エルジー ライフ サイエンス リミテッド | Sustained release composition of protein drug |
-
1990
- 1990-06-11 JP JP15360090A patent/JPH0446200A/en active Pending
Cited By (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2008530204A (en) * | 2005-02-21 | 2008-08-07 | エルジー ライフ サイエンス リミテッド | Sustained release composition of protein drug |
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