JPS6317899A - Purification of haptoglobin - Google Patents
Purification of haptoglobinInfo
- Publication number
- JPS6317899A JPS6317899A JP16159086A JP16159086A JPS6317899A JP S6317899 A JPS6317899 A JP S6317899A JP 16159086 A JP16159086 A JP 16159086A JP 16159086 A JP16159086 A JP 16159086A JP S6317899 A JPS6317899 A JP S6317899A
- Authority
- JP
- Japan
- Prior art keywords
- haptoglobin
- foreign materials
- aqueous solution
- fraction
- supernatant
- 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
- 102000014702 Haptoglobin Human genes 0.000 title claims abstract description 23
- 108050005077 Haptoglobin Proteins 0.000 title claims abstract description 23
- 238000000746 purification Methods 0.000 title description 4
- 239000007864 aqueous solution Substances 0.000 claims abstract description 12
- RMAQACBXLXPBSY-UHFFFAOYSA-N silicic acid Chemical compound O[Si](O)(O)O RMAQACBXLXPBSY-UHFFFAOYSA-N 0.000 claims abstract description 9
- 235000012239 silicon dioxide Nutrition 0.000 claims abstract description 9
- 238000000034 method Methods 0.000 claims description 23
- 239000012535 impurity Substances 0.000 claims description 9
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 abstract description 11
- 238000003756 stirring Methods 0.000 abstract description 5
- 239000003463 adsorbent Substances 0.000 abstract description 3
- 102000004169 proteins and genes Human genes 0.000 abstract description 3
- 108090000623 proteins and genes Proteins 0.000 abstract description 3
- -1 silica gel Chemical compound 0.000 abstract description 3
- 239000005995 Aluminium silicate Substances 0.000 abstract description 2
- 239000005909 Kieselgur Substances 0.000 abstract description 2
- 102000004895 Lipoproteins Human genes 0.000 abstract description 2
- 108090001030 Lipoproteins Proteins 0.000 abstract description 2
- 235000012211 aluminium silicate Nutrition 0.000 abstract description 2
- 239000000440 bentonite Substances 0.000 abstract description 2
- 229910000278 bentonite Inorganic materials 0.000 abstract description 2
- SVPXDRXYRYOSEX-UHFFFAOYSA-N bentoquatam Chemical compound O.O=[Si]=O.O=[Al]O[Al]=O SVPXDRXYRYOSEX-UHFFFAOYSA-N 0.000 abstract description 2
- 239000004927 clay Substances 0.000 abstract description 2
- NLYAJNPCOHFWQQ-UHFFFAOYSA-N kaolin Chemical compound O.O.O=[Al]O[Si](=O)O[Si](=O)O[Al]=O NLYAJNPCOHFWQQ-UHFFFAOYSA-N 0.000 abstract description 2
- 239000000741 silica gel Substances 0.000 abstract description 2
- 229910002027 silica gel Inorganic materials 0.000 abstract description 2
- 239000000463 material Substances 0.000 abstract 5
- 239000008119 colloidal silica Substances 0.000 abstract 2
- 230000002378 acidificating effect Effects 0.000 abstract 1
- 235000012216 bentonite Nutrition 0.000 abstract 1
- 239000000391 magnesium silicate Substances 0.000 abstract 1
- 229910052919 magnesium silicate Inorganic materials 0.000 abstract 1
- 235000019792 magnesium silicate Nutrition 0.000 abstract 1
- 239000012264 purified product Substances 0.000 abstract 1
- 239000006228 supernatant Substances 0.000 description 12
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 10
- 239000000203 mixture Substances 0.000 description 8
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 7
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 7
- 235000011130 ammonium sulphate Nutrition 0.000 description 7
- 239000000872 buffer Substances 0.000 description 6
- 102000006734 Beta-Globulins Human genes 0.000 description 5
- 108010087504 Beta-Globulins Proteins 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- 210000004369 blood Anatomy 0.000 description 5
- 238000005119 centrifugation Methods 0.000 description 5
- 239000002244 precipitate Substances 0.000 description 5
- 102000002572 Alpha-Globulins Human genes 0.000 description 4
- 108010068307 Alpha-Globulins Proteins 0.000 description 4
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 4
- 239000005695 Ammonium acetate Substances 0.000 description 4
- XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 4
- 229940043376 ammonium acetate Drugs 0.000 description 4
- 235000019257 ammonium acetate Nutrition 0.000 description 4
- 238000005194 fractionation Methods 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- IYLLULUTZPKQBW-UHFFFAOYSA-N Acrinol Chemical compound CC(O)C(O)=O.C1=C(N)C=CC2=C(N)C3=CC(OCC)=CC=C3N=C21 IYLLULUTZPKQBW-UHFFFAOYSA-N 0.000 description 3
- 108010054147 Hemoglobins Proteins 0.000 description 3
- 102000001554 Hemoglobins Human genes 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 239000007858 starting material Substances 0.000 description 3
- 102000006395 Globulins Human genes 0.000 description 2
- 108010044091 Globulins Proteins 0.000 description 2
- 239000008351 acetate buffer Substances 0.000 description 2
- 239000007853 buffer solution Substances 0.000 description 2
- 229910052742 iron Inorganic materials 0.000 description 2
- 229920006395 saturated elastomer Polymers 0.000 description 2
- 238000001179 sorption measurement Methods 0.000 description 2
- 229910002012 Aerosil® Inorganic materials 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- NINIDFKCEFEMDL-UHFFFAOYSA-N Sulfur Chemical compound [S] NINIDFKCEFEMDL-UHFFFAOYSA-N 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- PGZIKUPSQINGKT-UHFFFAOYSA-N dialuminum;dioxido(oxo)silane Chemical compound [Al+3].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O.[O-][Si]([O-])=O PGZIKUPSQINGKT-UHFFFAOYSA-N 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 108010071602 haptoglobin-hemoglobin complex Proteins 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 238000005461 lubrication Methods 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 230000004060 metabolic process Effects 0.000 description 1
- 210000000865 mononuclear phagocyte system Anatomy 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 210000005239 tubule Anatomy 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 210000002700 urine Anatomy 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Abstract
Description
【発明の詳細な説明】 〔産業上の利用分野〕 本発明はハプトグロビンの精製方法に関する。[Detailed description of the invention] [Industrial application field] The present invention relates to a method for purifying haptoglobin.
〔従来技術・発明が解決しようとする問題点〕ハプトグ
ロビンは分子１８５．０００〜４００．０００のタンパ
ク質であって血中に遊離するヘモグロビンの代謝に重要
な役割を演する。血中に遊離した分子！ｉ６７．０００
のヘモグロビンは過剰になると腎糸球体を通して尿中に
排泄されるに至り、鉄分を消耗するばかりでなく腎細尿
管の障害を引き起こす。[Prior Art/Problems to be Solved by the Invention] Haptoglobin is a protein with molecules of 185,000 to 400,000 and plays an important role in the metabolism of hemoglobin released in the blood. Free molecules in the blood! i67.000
When excess hemoglobin occurs, it is excreted into the urine through the renal glomerulus, which not only depletes iron but also causes damage to the renal tubules.
ハプトグロビンはヘモグロビンと選択的に強固に結合し
、ハプトグロビン−ヘモグロビン複合体を形成し、主と
して肝臓の細網内皮系に容易に取り込まれ、ここで代謝
されることによって、鉄ゐ回収と共に腎障害の防止に関
する重要な機能を有している。Haptoglobin selectively and tightly binds to hemoglobin to form a haptoglobin-hemoglobin complex, which is easily taken into the reticuloendothelial system of the liver and metabolized there, thereby recovering iron and preventing renal damage. It has important functions related to
ハプトグロビンは、たとえばヒト血漿のα−およびβ−
グロブリン画分より抽出精製されることが知られている
（日本国特許第９５８７７４号）。Haptoglobin is e.g. α- and β-
It is known that it can be extracted and purified from the globulin fraction (Japanese Patent No. 958774).
ところで、当該画分には夾雑物（例えば、リポ蛋白など
）が含まれるために、当該画分の水溶液は混濁している
。そこで、この溶液を清澄化して、その後の操作を円滑
に進めることが必要となる。By the way, since the fraction contains impurities (for example, lipoproteins, etc.), the aqueous solution of the fraction is cloudy. Therefore, it is necessary to clarify this solution to facilitate subsequent operations.
この方法としては、ヒト血漿のα−およびβ−グロブリ
ン画分の水溶液にアクリノールを添加して夾雑物を沈澱
させ、上清を回収した後、アクリノールを除（ために通
掛または吸着処理を行う方法が開示されている（前述日
本国特許）。In this method, acrinol is added to an aqueous solution of α- and β-globulin fractions of human plasma to precipitate impurities, and after collecting the supernatant, passing or adsorption treatment is performed to remove acrinol. A method is disclosed (the Japanese patent mentioned above).
しかし、この方法は操作が複雑であり、効果も充分でな
かった。However, this method was complicated to operate and was not sufficiently effective.
かかる実情下に、本発明者らは、ハブトグロビンの新た
な精製方法について検討した結果、粗製ハプトグロビン
を含む水溶液、特にヒト血崇のα〜およびβ−グロブリ
ン画分を含む水溶液をコロイド珪酸に接触させ、その非
吸着画分を回収することにより、ハプトグロビンを容易
に精製できることを見出し、本発明を完成した。Under these circumstances, the present inventors investigated a new method for purifying habtoglobin, and found that an aqueous solution containing crude haptoglobin, especially an aqueous solution containing α- and β-globulin fractions of human blood, was brought into contact with colloidal silicic acid. discovered that haptoglobin could be easily purified by collecting its non-adsorbed fraction, and completed the present invention.
即ち、本発明は、ハプトグロビンおよび夾雑物を含有す
る水溶液をコロイド珪酸と接触処理し、夾雑物を吸着除
去し、非吸着画分を回収することからなるハプトグロビ
ンの精製方法に関する。That is, the present invention relates to a method for purifying haptoglobin, which comprises contacting an aqueous solution containing haptoglobin and impurities with colloidal silicic acid, adsorbing and removing the impurities, and collecting a non-adsorbed fraction.
（１）出発原料
本発明の処理対象となる出発原料はハプトグロビンおよ
び夾雑物を含有する水溶液であり、好適にはヒト血漿の
α−およびβ−グロブリン画分が例示される。(1) Starting material The starting material to be treated in the present invention is an aqueous solution containing haptoglobin and impurities, and preferred examples include α- and β-globulin fractions of human plasma.
これは具体的には、コーンのエタノール分画法による第
■、■−１またはＩＶ−４画分、あるいは硫支分画法に
よる硫安飽和３５〜５０％濃度沈澱画分などが挙げられ
る。Specific examples of this include the No. 1, 2-1, or IV-4 fractions obtained by Cohn's ethanol fractionation method, and the 35-50% ammonium sulfate saturated precipitate fraction obtained by the sulfur fractionation method.
（２）前処理
本発明は夾雑物を除去するためのコロイド珪酸との接触
処理に先立ち、好ましくは前処理を施す。(2) Pretreatment In the present invention, a pretreatment is preferably performed prior to the contact treatment with colloidal silicic acid for removing impurities.
その前処理工程としては例えば、
■当該画分をｐＨ６〜９の緩衝液で”！！濁した後に同
一緩衝液に対して透析する工程
■当該百分をｐ１１６〜９の緩衝液で懸濁した後に遠心
分離して不溶物を除去する工程
■当該画分をｐＨ６〜９の！１衝液で懸濁した後に９１
１４．５〜９の条件下、硫酸アンモニウムを３０〜３５
％飽和濃度（０，２３〜０．２７ｋｇ／ｊ！に相当）ま
で添加した後、遠心分離して上清を回収する工程
■当該画分をｐＨ６〜９の緩衝液で懸濁した後にｐＨ６
〜９の条件下、硫酸アンモニウムを４０〜５０％飽和ｔ
；度（０，３〜０．３８ｋｇ／εに相当）まで添加した
後、遠心分離して沈澱を回収する工程等を挙げることが
できる。これらは組合せて用いることもできる。The pretreatment steps include, for example: ■ A step in which the fraction is turbid with a buffer solution with a pH of 6 to 9 and then dialyzed against the same buffer. ■ A step in which the fraction is suspended in a buffer solution with a pH of 116 to 9. A step of subsequently centrifuging to remove insoluble matter ■ After suspending the fraction in a !1 buffer with a pH of 6 to 9,
Ammonium sulfate under conditions of 14.5 to 9 and 30 to 35
% saturation concentration (equivalent to 0.23 to 0.27 kg/j!), and then centrifuging to collect the supernatant. ■ After suspending the fraction in a pH 6 to 9 buffer, pH 6
Ammonium sulfate was saturated at 40-50% under the conditions of ~9.
Examples include a step in which the precipitate is recovered by centrifugation after addition to a temperature of 0.3 to 0.38 kg/ε. These can also be used in combination.
（３）本処理
（１）または（２）で得られるハプトグロビンを含む水
溶液、たとえばヒト血漿のα−およびβ−グロブリン画
分を含む溶液をコロイド珪酸と接触・混和させる。(3) The aqueous solution containing haptoglobin obtained in treatment (1) or (2), for example, the solution containing α- and β-globulin fractions of human plasma, is brought into contact with and mixed with colloidal silicic acid.
吸着剤として用いられるコロイド珪酸としては、シリカ
ゲル、軽質無水珪酸、ケイソウ土、酸性白土、ベントナ
イト、カオリン、珪酸アルミン酸マグネシウムなどが挙
げられる。好適には軽質無水珪酸が用いられる。Examples of colloidal silicic acid used as an adsorbent include silica gel, light anhydrous silicic acid, diatomaceous earth, acid clay, bentonite, kaolin, and magnesium aluminate silicate. Light silicic anhydride is preferably used.
また、接触条件としては、蛍白濃度１〜１００ｇ／ｌ（
好ましくは１０〜１００ｇ／ｆｆ１）、吸着剤量１〜３
０ｇ／ｌ、ｐＨ４〜９ （好ましくはｐＨ６〜８）など
が挙げられる。In addition, the contact conditions include a fluorescent white concentration of 1 to 100 g/l (
Preferably 10-100g/ff1), adsorbent amount 1-3
0 g/l, pH 4 to 9 (preferably pH 6 to 8), and the like.
本処理はバッチ法、カラム法のどちらでも行われうるが
、好ましくはバッチ法を用いる。This treatment can be carried out by either a batch method or a column method, but preferably a batch method is used.
バッチ法の場合の条件としては、５〜２５℃、５分〜１
時間程度、混和、撹拌される。The conditions for the batch method are 5 to 25°C, 5 minutes to 1
Mix and stir for about an hour.
その後、濾過または遠心分離により上清（非吸着画分）
を回収する。この吸着処理によりリボプロティン、αｌ
−グロブリン等が除去される。The supernatant (non-adsorbed fraction) is then filtered or centrifuged.
Collect. Through this adsorption treatment, riboprotein, αl
- Globulins etc. are removed.
（４）製剤化
本発明の精製方法は、ハプトグロビンの公知の精製方法
の一工程として４入することも可能である。例えば、限
外濾過、陰イオン交換体処理、硫安分画などの方法と組
み合わせることにより、高度精製を行い、さらに公知の
製剤化技術を組み合わせることにより、臨床上適用でき
るハプトグロビン製剤を堤供することができる。(4) Formulation The purification method of the present invention can also be formulated into four formulations as one step of a known purification method for haptoglobin. For example, by combining methods such as ultrafiltration, anion exchanger treatment, and ammonium sulfate fractionation, it is possible to achieve a high degree of purification, and by further combining known formulation techniques, it is possible to provide clinically applicable haptoglobin preparations. can.
［効果〕
本発明の方法によれば、従来法（アクリノール法）に比
べて簡単な処理でハプトグロビン含有水溶液中の夾雑物
を除去することができる。[Effects] According to the method of the present invention, impurities in a haptoglobin-containing aqueous solution can be removed with a simpler treatment than the conventional method (acrinol method).
〔実施例〕
本発明をより詳細に説明するために実施例を挙げるが、
本発明はこれらによって限定されるものではない。[Example] Examples will be given to explain the present invention in more detail.
The present invention is not limited to these.
実施例１
人血漿よりコーンの低温エタノール分画法で得た百分Ｉ
Ｖ ３０ ｋｇにｐｌ！８．２の０．０５モル酢酸アン
モニウム緩衝液１４５１を加え懸濁した。これに軽質無
水珪酸（第９改正日本薬局方）１ｋｇを加え、室温で１
時間攪拌した後、遠心分離して上清を回収した。この上
清中にハプトグロビンは９５％回収されていた。本処理
により主としてリボ蛋白が除かれ、純度が向上するとと
もに清澄な液が得られた。Example 1 Percent I obtained from human plasma by Cohn's low-temperature ethanol fractionation method
V 30 kg pl! 8.2 of 0.05M ammonium acetate buffer 1451 was added and suspended. Add 1 kg of light silicic anhydride (9th edition Japanese Pharmacopoeia) to this and
After stirring for an hour, the mixture was centrifuged and the supernatant was collected. 95% of haptoglobin was recovered in this supernatant. This treatment mainly removed riboproteins, improving purity and producing a clear liquid.
実施例２
人血齋をコーンのエタノール法で分画して得た画分ＩＶ
３ ｋｇをｐＨ７の０．０５Ｍ酢酸緩衝液１５１中に
懸濁した後、酢酸緩衝液に対して透析し、エタノールを
除き、不溶物を遠心分離して除去した。Example 2 Fraction IV obtained by fractionating human blood using Cohn's ethanol method
After suspending 3 kg in 0.05M acetate buffer 151 at pH 7, it was dialyzed against acetate buffer to remove ethanol, and insoluble materials were removed by centrifugation.
得られた上澄液に、３３％飽和となるように硫酸アンモ
ニウムを加え、生じた沈澱を遠心分離で除去した後、硫
酸アンモニウムを追加して飽和度を４０％とした。生じ
た沈澱を濾別採取し、水１０１に溶解した後、軽質無水
珪酸５０ｇを加え、室温で１時間攪拌した後、遠心分離
して上清を回収した。この上清中にハプトグロビンは７
０％回収されていた。本処理により、αｌ−グロブリン
、β−グロブリン、アルブミン、リボ蛋白等の不要蛋白
が除かれ、純度が向上するとともに清澄な液を得ること
ができた。Ammonium sulfate was added to the obtained supernatant so that the degree of saturation was 33%, and the resulting precipitate was removed by centrifugation, and then ammonium sulfate was added to bring the degree of saturation to 40%. The resulting precipitate was collected by filtration, dissolved in 10 ml of water, 50 g of light anhydrous silicic acid was added, and after stirring at room temperature for 1 hour, the mixture was centrifuged to collect the supernatant. There are 7 haptoglobin in this supernatant.
0% was recovered. By this treatment, unnecessary proteins such as αl-globulin, β-globulin, albumin, and riboprotein were removed, and purity was improved and a clear liquid could be obtained.
実施例３
新規なプール血＝ｔｏｆｆから硫酸アンモニウム沈澱法
により得たα−１β−グロブリン画分を出発原料として
用いた。これに酢酸アンモニウムを加えてｐＨ１８の酢
酸アンモニウム緩衝液１０１を加え懸眉液となし、軽質
無水珪酸５０ｇを加え、室温で１時間攪拌した後、遠心
分離して上清を回収した。この上清中にハプトグロビン
は９５％回収されていた。本処理により、主としてリボ
蛋白が除かれ、純度が向上するとともに清澄な液を得る
ことができた。Example 3 An α-1β-globulin fraction obtained from a new pool of blood (toff) by ammonium sulfate precipitation was used as a starting material. To this was added ammonium acetate and ammonium acetate buffer 101 having a pH of 18 to obtain a suspension solution, 50 g of light silicic anhydride was added, and after stirring at room temperature for 1 hour, the mixture was centrifuged to collect the supernatant. 95% of haptoglobin was recovered in this supernatant. Through this treatment, riboproteins were mainly removed, the purity was improved, and a clear liquid could be obtained.
実施例４
大血漿をコーンのエタノール法で分画して得た画分１’
Ｖ ３０ ｋｇをｐｕｓ、２の０．０５ Ｍ酢酸アンモ
ニウム緩衝液１４０１に懸濁した後、硫酸アンモニウム
を３５％飽和となるように加え、生じた沈澱を遠心分離
して除いた。この上清をｐＨ７，５に調整した後、軽質
無水珪酸〔アエロジル（ジグサ社製）〕ｌ ｋｇを加え
、室温で１時間攪拌した。その後に遠心分離して上清を
回収した。上滑中にハプトグロビンは７０％回収され、
溶液の濁りも完全に除去できた。Example 4 Fraction 1' obtained by fractionating large plasma using Cohn's ethanol method
After suspending 30 kg of V in 0.05 M ammonium acetate buffer 1401 at pus, 2, ammonium sulfate was added to achieve 35% saturation, and the resulting precipitate was removed by centrifugation. After adjusting the pH of this supernatant to 7.5, 1 kg of light silicic anhydride [Aerosil (manufactured by Jigusa Corporation)] was added, and the mixture was stirred at room temperature for 1 hour. Thereafter, the supernatant was collected by centrifugation. 70% of haptoglobin was recovered during the lubrication process,
The turbidity of the solution was also completely removed.
Claims (1)
ド珪酸と接触処理し、夾雑物を吸着除去し、非吸着画分
を回収することからなるハプトグロビンの精製方法。A method for purifying haptoglobin, which comprises contacting an aqueous solution containing haptoglobin and impurities with colloidal silicic acid, adsorbing and removing the impurities, and collecting a non-adsorbed fraction.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP16159086A JPS6317899A (en) | 1986-07-09 | 1986-07-09 | Purification of haptoglobin |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP16159086A JPS6317899A (en) | 1986-07-09 | 1986-07-09 | Purification of haptoglobin |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPS6317899A true JPS6317899A (en) | 1988-01-25 |
Family
ID=15738025
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP16159086A Pending JPS6317899A (en) | 1986-07-09 | 1986-07-09 | Purification of haptoglobin |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS6317899A (en) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0944392A1 (en) * | 1996-07-01 | 1999-09-29 | Alpha Therapeutic Corporation | Process for separating alpha-1-proteinase inhibitor from cohn fraction iv 1? +iv 4? paste |
| WO2006109405A1 (en) * | 2005-04-07 | 2006-10-19 | Asahi Breweries, Ltd. | Method for preparation of plant extract |
| JP2015532301A (en) * | 2012-10-03 | 2015-11-09 | シーエスエル・ベーリング・エルエルシー | Protein purification method |
| US9534029B2 (en) | 2012-10-03 | 2017-01-03 | Csl Behring Ag | Method of purifying proteins |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5182716A (en) * | 1974-12-14 | 1976-07-20 | Biotest Serum Institut Gmbh | 1 tsunogenryokarairyonishoshiuru 3 shunoseiseibutsuodojiniseizosuruhoho |
| JPS55100319A (en) * | 1979-01-20 | 1980-07-31 | Biotest Serum Institut Gmbh | Plasma fractration stabilized by citrate |
| JPS59118710A (en) * | 1982-12-21 | 1984-07-09 | ビオテスト アクチエンゲゼルシャフト | Coagulation-active plasma protein solution, manufacture and medicine |
-
1986
- 1986-07-09 JP JP16159086A patent/JPS6317899A/en active Pending
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS5182716A (en) * | 1974-12-14 | 1976-07-20 | Biotest Serum Institut Gmbh | 1 tsunogenryokarairyonishoshiuru 3 shunoseiseibutsuodojiniseizosuruhoho |
| JPS55100319A (en) * | 1979-01-20 | 1980-07-31 | Biotest Serum Institut Gmbh | Plasma fractration stabilized by citrate |
| JPS59118710A (en) * | 1982-12-21 | 1984-07-09 | ビオテスト アクチエンゲゼルシャフト | Coagulation-active plasma protein solution, manufacture and medicine |
Cited By (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0944392A1 (en) * | 1996-07-01 | 1999-09-29 | Alpha Therapeutic Corporation | Process for separating alpha-1-proteinase inhibitor from cohn fraction iv 1? +iv 4? paste |
| AU726233B2 (en) * | 1996-07-01 | 2000-11-02 | Baxalta GmbH | Process for separating alpha-1-proteinase inhibitor from cohn fraction IV1+IV4 paste |
| EP0944392A4 (en) * | 1996-07-01 | 2004-11-24 | Alpha Therapeutic Corp | Process for separating alpha-1-proteinase inhibitor from cohn fraction iv 1? +iv 4? paste |
| EP1762576A1 (en) * | 1996-07-01 | 2007-03-14 | Baxter International Inc. | Process for separating alpha-1-proteinase inhibitor from Cohn Fraction IV1+IV4 paste |
| CZ300452B6 (en) * | 1996-07-01 | 2009-05-20 | Alpha Therapeutic Corporation | Process for purifying alpha-1-proteinase inhibitor |
| CZ301332B6 (en) * | 1996-07-01 | 2010-01-20 | Alpha Therapeutic Corporation | Process for removing apolipoprotein from protein solution |
| WO2006109405A1 (en) * | 2005-04-07 | 2006-10-19 | Asahi Breweries, Ltd. | Method for preparation of plant extract |
| JP2015532301A (en) * | 2012-10-03 | 2015-11-09 | シーエスエル・ベーリング・エルエルシー | Protein purification method |
| US9534029B2 (en) | 2012-10-03 | 2017-01-03 | Csl Behring Ag | Method of purifying proteins |
| US9937229B2 (en) | 2012-10-03 | 2018-04-10 | Csl Behring Ag | Methods of treatment using hemopexin compositions |
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