JPH04108341A - Method for improving blood plasma - Google Patents
Method for improving blood plasmaInfo
- Publication number
- JPH04108341A JPH04108341A JP2224266A JP22426690A JPH04108341A JP H04108341 A JPH04108341 A JP H04108341A JP 2224266 A JP2224266 A JP 2224266A JP 22426690 A JP22426690 A JP 22426690A JP H04108341 A JPH04108341 A JP H04108341A
- Authority
- JP
- Japan
- Prior art keywords
- plasma
- protein
- adsorbent
- concentration
- adjusted
- 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
- 238000000034 method Methods 0.000 title claims abstract description 15
- 210000002381 plasma Anatomy 0.000 title abstract 5
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 30
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 30
- 239000003463 adsorbent Substances 0.000 claims abstract description 14
- 239000007788 liquid Substances 0.000 claims abstract description 6
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 abstract description 14
- 238000011084 recovery Methods 0.000 abstract description 11
- 239000000126 substance Substances 0.000 abstract description 5
- 102000004506 Blood Proteins Human genes 0.000 abstract description 4
- 108010017384 Blood Proteins Proteins 0.000 abstract description 4
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 abstract description 4
- 229920002125 Sokalan® Polymers 0.000 abstract description 2
- 235000010443 alginic acid Nutrition 0.000 abstract description 2
- 239000000783 alginic acid Substances 0.000 abstract description 2
- 229960001126 alginic acid Drugs 0.000 abstract description 2
- 229920000615 alginic acid Polymers 0.000 abstract description 2
- 150000004781 alginic acids Chemical class 0.000 abstract description 2
- 230000007935 neutral effect Effects 0.000 abstract description 2
- 239000004584 polyacrylic acid Substances 0.000 abstract description 2
- 238000004040 coloring Methods 0.000 abstract 1
- 239000000377 silicon dioxide Substances 0.000 abstract 1
- 102000001554 Hemoglobins Human genes 0.000 description 8
- 108010054147 Hemoglobins Proteins 0.000 description 8
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 8
- 238000001914 filtration Methods 0.000 description 7
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 6
- 210000004369 blood Anatomy 0.000 description 5
- 239000008280 blood Substances 0.000 description 5
- 230000000052 comparative effect Effects 0.000 description 4
- IXPNQXFRVYWDDI-UHFFFAOYSA-N 1-methyl-2,4-dioxo-1,3-diazinane-5-carboximidamide Chemical compound CN1CC(C(N)=N)C(=O)NC1=O IXPNQXFRVYWDDI-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 239000000661 sodium alginate Substances 0.000 description 3
- 235000010413 sodium alginate Nutrition 0.000 description 3
- 229940005550 sodium alginate Drugs 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 210000000601 blood cell Anatomy 0.000 description 2
- 235000013305 food Nutrition 0.000 description 2
- 235000013373 food additive Nutrition 0.000 description 2
- 239000002778 food additive Substances 0.000 description 2
- BTIJJDXEELBZFS-QDUVMHSLSA-K hemin Chemical compound CC1=C(CCC(O)=O)C(C=C2C(CCC(O)=O)=C(C)\C(N2[Fe](Cl)N23)=C\4)=N\C1=C/C2=C(C)C(C=C)=C3\C=C/1C(C)=C(C=C)C/4=N\1 BTIJJDXEELBZFS-QDUVMHSLSA-K 0.000 description 2
- 229940025294 hemin Drugs 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- RMAQACBXLXPBSY-UHFFFAOYSA-N silicic acid Chemical compound O[Si](O)(O)O RMAQACBXLXPBSY-UHFFFAOYSA-N 0.000 description 2
- 235000012239 silicon dioxide Nutrition 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 239000008399 tap water Substances 0.000 description 2
- 235000020679 tap water Nutrition 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 206010018910 Haemolysis Diseases 0.000 description 1
- 239000005909 Kieselgur Substances 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- OHJMTUPIZMNBFR-UHFFFAOYSA-N biuret Chemical compound NC(=O)NC(N)=O OHJMTUPIZMNBFR-UHFFFAOYSA-N 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000004927 clay Substances 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- SHFGJEQAOUMGJM-UHFFFAOYSA-N dialuminum dipotassium disodium dioxosilane iron(3+) oxocalcium oxomagnesium oxygen(2-) Chemical compound [O--].[O--].[O--].[O--].[O--].[O--].[O--].[O--].[Na+].[Na+].[Al+3].[Al+3].[K+].[K+].[Fe+3].[Fe+3].O=[Mg].O=[Ca].O=[Si]=O SHFGJEQAOUMGJM-UHFFFAOYSA-N 0.000 description 1
- HNPSIPDUKPIQMN-UHFFFAOYSA-N dioxosilane;oxo(oxoalumanyloxy)alumane Chemical compound O=[Si]=O.O=[Al]O[Al]=O HNPSIPDUKPIQMN-UHFFFAOYSA-N 0.000 description 1
- 230000000694 effects Effects 0.000 description 1
- 230000008588 hemolysis Effects 0.000 description 1
- 238000009776 industrial production Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 239000010451 perlite Substances 0.000 description 1
- 235000019362 perlite Nutrition 0.000 description 1
- 229920001495 poly(sodium acrylate) polymer Polymers 0.000 description 1
- 239000005518 polymer electrolyte Substances 0.000 description 1
- 238000003672 processing method Methods 0.000 description 1
- 235000013580 sausages Nutrition 0.000 description 1
- -1 silica gel Chemical compound 0.000 description 1
- 239000000741 silica gel Substances 0.000 description 1
- 229910002027 silica gel Inorganic materials 0.000 description 1
- NNMHYFLPFNGQFZ-UHFFFAOYSA-M sodium polyacrylate Chemical compound [Na+].[O-]C(=O)C=C NNMHYFLPFNGQFZ-UHFFFAOYSA-M 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Meat, Egg Or Seafood Products (AREA)
Abstract
Description
【発明の詳細な説明】 （産業上の利用分野） 本発明は、血漿の改良方法に関するものである。[Detailed description of the invention] (Industrial application field) The present invention relates to a method for improving plasma.
（従来の技術）
血液は遠心分離することにより、血球成分と血漿成分に
分けられる。この血漿成分は加熱するとゲル化するとい
う特性を持っているので、ハム、ソーセージなどの食品
添加物として利用されている。(Prior Art) Blood is separated into blood cell components and plasma components by centrifugation. This plasma component has the property of turning into a gel when heated, so it is used as a food additive for foods such as ham and sausage.
従来、血漿は遠心分離した後、チルドの状態で使用され
たり、そのままスプレードライなどの方法で乾燥して使
用されている。しかし、産業的に通常利用されている血
漿は、加熱してゲル化させると、得られるゲルが着色し
ていたり、異臭がするという問題点があり、そのため利
用が限られている。Conventionally, plasma has been centrifuged and then used in a chilled state, or directly dried by a method such as spray drying. However, plasma that is commonly used industrially has the problem that when it is heated to gel, the resulting gel is colored and has a strange odor, which limits its use.
そこで血漿の用途を広げるために、異臭及び着色の原因
物質を除去する方法が期待されている。Therefore, in order to expand the uses of plasma, a method for removing substances that cause off-odor and coloration is expected.
（発明が解決しようとする課題）
本発明の目的は、簡単な操作により、異臭及び着色物質
の少ない血漿由来の蛋白質を、回収率良く、濾過速度が
早く、吸着剤の除去効率を向上し、工業的有利に生産す
ることができる処理方法を提供することにある。(Problems to be Solved by the Invention) The purpose of the present invention is to obtain plasma-derived proteins with low off-odor and colored substances through simple operations, with a high recovery rate, a fast filtration rate, and an improved adsorbent removal efficiency. It is an object of the present invention to provide a processing method that allows industrially advantageous production.
（課題を解決するための手段）
本発明者らはすでに血漿の改良方法について検討を行い
特許出願している（特願昭８３−２９０１０７、特願昭
６３−２９０１０８ 、特願昭８３−３１２９６３ 、
特願平ｌ−３８２９３、特願平１−３８２９４ 、特願
平１−７０５０２、特願平１−７０５０３ 、特願平１
−１５１５３８、特願平１−２１６０２０）。(Means for Solving the Problems) The present inventors have already studied and applied for patents on a method for improving plasma (Japanese Patent Application No. 83-290107, Japanese Patent Application No. 63-290108, Japanese Patent Application No. 83-312963,
Japanese Patent Application No. 1-38293, Japanese Patent Application No. 1-38294, Japanese Patent Application No. 1-70502, Japanese Patent Application No. 1-70503, Japanese Patent No. 1-1
-151538, patent application No. 1-216020).
しかし工業的に生産することに関しては血漿蛋白質の回
収率が悪い、濾過速度が遅い、吸着剤の除去効率を向上
させなければならないといった課題が残されていた。However, when it comes to industrial production, there remain problems such as poor recovery of plasma proteins, slow filtration rate, and the need to improve the removal efficiency of the adsorbent.
本発明者らは、さらに鋭意検討した結果、血漿を特定の
蛋白質濃度、特定の液温、特定のｐＨに調整し、吸着剤
を用いて処理することにより工業的に適した血漿蛋白質
を得ることを見い出だし、本発明を完成するに至った。As a result of further intensive studies, the present inventors have found that industrially suitable plasma proteins can be obtained by adjusting plasma to a specific protein concentration, specific liquid temperature, and specific pH, and treating it with an adsorbent. They discovered this and completed the present invention.
すなわち本発明は、血漿を、蛋白質濃度が２〜５％、液
温か２０〜３０℃、ｐ１１３〜５の条件下、吸着剤と接
触させ、血漿の改良を行うことを特徴とする血漿の改良
方法である。以下、本発明の詳細な説明する。That is, the present invention provides a method for improving plasma, which is characterized in that the plasma is improved by contacting the plasma with an adsorbent under conditions of a protein concentration of 2 to 5%, a liquid temperature of 20 to 30°C, and a p113 to 5 condition. It is. The present invention will be explained in detail below.
本発明に使用する血漿は動物の血液より得られたものを
使用する。このとき溶血等により血球成分が血漿中に含
まれていても、−向に差し支えない。The plasma used in the present invention is obtained from animal blood. At this time, even if blood cell components are contained in the plasma due to hemolysis or the like, there is no problem in the negative direction.
血漿中の蛋白質濃度については、血漿溶液を水等により
希釈し、蛋白質濃度２〜５％、好ましくは３〜４％に調
整し、吸着剤を用いて処理する。Regarding the protein concentration in plasma, the plasma solution is diluted with water or the like to adjust the protein concentration to 2 to 5%, preferably 3 to 4%, and then treated using an adsorbent.
それは、通常、産業的に作られる血漿の蛋白質濃度は６
〜８％程度であり、その濃度のまま吸着剤を用いて処理
すると濃度が高すぎるため、蛋白質が変性しやすく、用
いた吸着剤の濾別が非常に困難になり、吸着剤の除去効
率や蛋白回収率か悪くなるからである。従って蛋白質濃
度の上限は５９゜である。一方、蛋白質濃度が低すぎる
と処理効率が悪いため、その下限は２％である。The protein concentration of industrially produced plasma is usually 6
The concentration is about ~8%, and if treated with an adsorbent at that concentration, the concentration will be too high, and the protein will easily denature, making it extremely difficult to filter out the adsorbent used, and reducing the removal efficiency of the adsorbent. This is because the protein recovery rate will be poor. Therefore, the upper limit of protein concentration is 59°. On the other hand, if the protein concentration is too low, the processing efficiency will be poor, so the lower limit is 2%.
処理温度については、血漿中に含まれているアルブミン
が熱変性せず、かつ、ヘモグロビンが変性しやすい温度
、即ち２０〜３０℃で処理する。通常、雑菌の増殖や、
蛋白質の変性を防ぐために４℃程度の低温で処理するこ
とが多いが、それてはヘモグロビンの除去効率が悪いか
らである。Regarding the treatment temperature, the treatment is performed at a temperature at which albumin contained in plasma is not thermally denatured and hemoglobin is easily denatured, that is, 20 to 30°C. Usually, the growth of bacteria,
In order to prevent protein denaturation, processing is often carried out at a low temperature of about 4°C, but this is because hemoglobin removal efficiency is low.
ｐｌについては３〜５で処理する。それは、ヘモグロビ
ンの除去効率かよく、雑菌の増殖も防げるからである。Regarding pl, process 3 to 5. This is because it has high hemoglobin removal efficiency and prevents the growth of bacteria.
ｐｎ調整には、塩酸、燐酸、酢酸など、得られた血漿を
食品添加物として使用する場合を考慮して、食品製造工
程上使用が認められているものを用いることが望ましい
。For pn adjustment, it is desirable to use hydrochloric acid, phosphoric acid, acetic acid, etc. that are approved for use in food manufacturing processes, considering the use of the obtained plasma as a food additive.
次にここで用いられる吸着剤としては、例えば活性炭、
コロイド珪酸（例えば、シリカゲル、軽質無水珪酸、酸
性白土）、パーライト、ラジオライト、けいそう土等が
あげられ、その使用量は血漿の接触時間や蛋白質回収率
との兼ね合いによるが、約０．５〜３０％好ましくは、
５〜２０％である。Next, as the adsorbent used here, for example, activated carbon,
Examples include colloidal silicic acid (e.g. silica gel, light anhydrous silicic acid, acid clay), perlite, radiolite, diatomaceous earth, etc. The amount used depends on the balance with plasma contact time and protein recovery rate, but is approximately 0.5 ~30% preferably
It is 5-20%.
また吸着剤としてカルボキシル基を有する高分子電解質
（例えば、アルギン酸、アルギン酸ナトリウム、ポリア
クリル酸、ポリアクリル酸ナトリウム、カルボキシメチ
ルセルロース）なども用いられ、その使用量は約０．０
０１〜０．２％である。吸着剤は２種以上組み合わせて
用いることもできる。Polymer electrolytes having carboxyl groups (e.g., alginic acid, sodium alginate, polyacrylic acid, sodium polyacrylate, carboxymethylcellulose) are also used as adsorbents, and the amount used is approximately 0.0
01-0.2%. Two or more kinds of adsorbents can also be used in combination.
血漿との接触のさせ方には特に限定はなく、バッチ法、
カラム法いずれの方法も使用できる。There are no particular restrictions on the method of contact with plasma; batch methods,
Any column method can be used.
以上のようにして得られた改良血漿溶液は、必要に応じ
てｐＨを中性領域に戻したり、濃縮したりすれば良い。The improved plasma solution obtained as described above may be returned to a neutral pH range or concentrated as necessary.
（発明の効果）
本発明の方法で処理することにより、異臭及び着色物質
の少ない血漿蛋白質を、工業的に適した方法で回収率良
く得ることかできる。即ち本発明方法によればヘモグロ
ビン濃度が約０．０４０未満で、悪臭及び着色物質の少
ない改良血漿を、蛋白質回収率が約８５％以上と高い回
収率で得ることができる。(Effects of the Invention) By processing according to the method of the present invention, plasma proteins with less off-odor and colored substances can be obtained with a high recovery rate by an industrially suitable method. That is, according to the method of the present invention, improved plasma having a hemoglobin concentration of less than about 0.040 and less malodor and colored substances can be obtained with a high protein recovery rate of about 85% or more.
（実施例）
以下実施例により本発明を更に詳細に説明するが、本発
明はこれらの実施例のみに限定されるものではない。(Examples) The present invention will be explained in more detail with reference to Examples below, but the present invention is not limited to these Examples.
各実施例において、蛋白質含量はビュウレット試薬で定
量し、又、ヘモグロビン含量は４１０ ｎｍのヘミンの
吸光度をｎｊ定することにより求めた。又、蛋白質中の
ヘモグロビン濃度は、ヘミン吸光度（Ａ）と蛋白質濃度
（ｍｇ／ｍｌ、 （Ｂ））との比（Ａ）／ （Ｂ）と
して表した。In each Example, the protein content was determined using Biuret's reagent, and the hemoglobin content was determined by determining the absorbance of hemin at 410 nm. Further, the hemoglobin concentration in the protein was expressed as the ratio (A)/(B) of the hemin absorbance (A) and the protein concentration (mg/ml, (B)).
実施例１．２、比較例１〜１３
豚の血液を遠心分離して血漿を得た後、その血漿を膜濃
縮や水道水で希釈することにより、各濃度の豚血漿（蛋
白質ｕ ｍ １ｆｌｉ９０％ １１９ｃｉ ％ ８９６
．５９ｏ１２９ｏ）を調整した。Example 1.2, Comparative Examples 1 to 13 After centrifuging pig blood to obtain plasma, the plasma was membrane concentrated or diluted with tap water to obtain pig plasma of various concentrations (protein um 1fli 90%). 119ci% 896
．． 59o129o) were adjusted.
上記のように調整したサンプルの液温を、５℃、１５℃
、２５℃に調整した後、それぞれのサンプルの蛋白質量
に対して活性炭を２０重量％、アルギン酸ナトリウムを
０．２重−％加えた後、塩酸を加えることによりｐＨを
４に調整した。そのままの状態で、５時間攪拌した後、
加えた活性炭や沈澱物を濾別除去した。得られた溶液に
水酸化ナトリウムを加えることによりｐＨを７に調整し
た。このようにして得られたおのおののサンプルの処理
前、処理後の上滑の蛋白質量及びヘモグロビン量を測定
した。The liquid temperature of the sample adjusted as above was adjusted to 5°C and 15°C.
After adjusting the temperature to 25° C., 20% by weight of activated carbon and 0.2% by weight of sodium alginate were added to the protein amount of each sample, and the pH was adjusted to 4 by adding hydrochloric acid. After stirring for 5 hours,
The added activated carbon and precipitate were removed by filtration. The pH was adjusted to 7 by adding sodium hydroxide to the resulting solution. The amount of protein and hemoglobin in the upper layer of each sample thus obtained was measured before and after treatment.
又、処理前の蛋白質量を１００％として、処理後の蛋白
回収率を求めた。その結果を表１にまとめた。In addition, the protein recovery rate after treatment was determined by setting the amount of protein before treatment as 100%. The results are summarized in Table 1.
表１から明らかなように、実施例では蛋白回収率も良く
、ヘモグロン濃度も低値の改良血漿が得られた。As is clear from Table 1, improved plasma with good protein recovery and low hemoglone concentration was obtained in the Examples.
実施例３，４、比較例１４〜１６
豚の血液を遠心分離して血漿を得た後、その血漿を膜濃
縮や水道水で希釈することにより、各濃度の豚血漿（蛋
白質ａ ｍ １６９６．１１９ｏ、 ８９ｏ、５９ｏ１
２９ｏ）を調整した。Examples 3 and 4, Comparative Examples 14 to 16 Pig blood was centrifuged to obtain plasma, and then the plasma was membrane concentrated or diluted with tap water to obtain various concentrations of pig plasma (protein am 1696. 119o, 89o, 59o1
29o) was adjusted.
上記のように調整したサンプル５００ ｍｌに塩酸を加
えることによりｐＩ（を４に調整し、活性炭２０９ｏを
加え、２５℃で室温で３時間攪拌した。沈澱物を濾別す
るためにフィルターペーパー（直径１２．５ｃｍ）でブ
フナー濾過を行った。サンプル５００ｍ１の濾過終了ま
でに要する時間を比較した。結果を表２に示す。表２か
ら明らかなように、実施例では濾過時間が短く、操作が
簡便であった。The pI (pI) was adjusted to 4 by adding hydrochloric acid to 500 ml of the sample prepared as above, activated carbon 209° was added, and the mixture was stirred at 25°C and room temperature for 3 hours. Buchner filtration was performed using a filter with a diameter of 12.5 cm.The time required to complete the filtration of 500 ml of sample was compared.The results are shown in Table 2.As is clear from Table 2, the filtration time was short in the example, and the operation was simple. Met.
実施例５，６、比較例１７
豚の血液を遠心分離して血漿（比較例１７）を得た後、
その血漿を０．０１％アルギン酸ナトリウム溶液で蛋白
質濃度４％（実施例５）、２％（実施例６）に調整した
。Examples 5 and 6, Comparative Example 17 After centrifuging pig blood to obtain plasma (Comparative Example 17),
The plasma was adjusted to a protein concentration of 4% (Example 5) and 2% (Example 6) with a 0.01% sodium alginate solution.
上記のように調整したサンプルの液温を、２５℃に調整
した後、それぞれのサンプルの蛋白質量に対して活性炭
を３０重量９６加えた後、塩酸を加えることによりｐＨ
を４に調整した。そのままの状態で、５時間攪拌した後
、加えた活性炭や沈澱物を濾別除去した。得られた溶液
に水酸化ナトリウムを加えることによりｐＨを７に調整
した。このようにして得られたおのおののサンプルの処
理前、処理後の上滑の蛋白質量及びヘモグロビン量を測
定した。After adjusting the liquid temperature of the samples adjusted as above to 25℃, activated carbon was added at 30% by weight based on the protein amount of each sample, and then the pH was adjusted by adding hydrochloric acid.
was adjusted to 4. After stirring as it was for 5 hours, the added activated carbon and precipitate were removed by filtration. The pH was adjusted to 7 by adding sodium hydroxide to the resulting solution. The amount of protein and hemoglobin in the upper layer of each sample thus obtained was measured before and after treatment.
又、処理前の蛋白質量を１００％として、処理後の蛋白
回収率を求めた。その結果を表３にまとめた。In addition, the protein recovery rate after treatment was determined by setting the amount of protein before treatment as 100%. The results are summarized in Table 3.
表３から明らかなように、実施例では蛋白回収率も良く
、ヘモグロン濃度も低値の改良血漿が得られた。As is clear from Table 3, in the Examples, improved plasma with good protein recovery and low hemoglone concentration was obtained.
Claims (1)
ｐＨ３〜５の条件下、吸着剤と接触させ、血漿の改良を
行うことを特徴とする血漿の改良方法。Plasma has a protein concentration of 2 to 5%, a liquid temperature of 20 to 30°C,
A method for improving plasma, which comprises improving plasma by bringing it into contact with an adsorbent under conditions of pH 3 to 5.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2224266A JPH04108341A (en) | 1990-08-28 | 1990-08-28 | Method for improving blood plasma |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP2224266A JPH04108341A (en) | 1990-08-28 | 1990-08-28 | Method for improving blood plasma |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH04108341A true JPH04108341A (en) | 1992-04-09 |
Family
ID=16811085
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2224266A Pending JPH04108341A (en) | 1990-08-28 | 1990-08-28 | Method for improving blood plasma |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH04108341A (en) |
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2000504569A (en) * | 1996-02-09 | 2000-04-18 | ソシエテ デ プロデユイ ネツスル ソシエテ アノニム | Ice crystal growth inhibitor |
| US7495416B2 (en) | 2003-11-14 | 2009-02-24 | Sony Corporation | Battery pack, battery protection processing apparatus, and startup control method of the battery protection processing apparatus |
-
1990
- 1990-08-28 JP JP2224266A patent/JPH04108341A/en active Pending
Cited By (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2000504569A (en) * | 1996-02-09 | 2000-04-18 | ソシエテ デ プロデユイ ネツスル ソシエテ アノニム | Ice crystal growth inhibitor |
| US7495416B2 (en) | 2003-11-14 | 2009-02-24 | Sony Corporation | Battery pack, battery protection processing apparatus, and startup control method of the battery protection processing apparatus |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US4170590A (en) | Ion exchanger treatment of citrate-stabilized plasma | |
| US4081431A (en) | Blood fractionation | |
| EP0397890B1 (en) | Process for purifying blood plasma | |
| Gea et al. | Continuous production of high degree casein hydrolysates by immobilized proteases in column reactor | |
| US4348482A (en) | Process for decreasing the thermal stability of microbial rennet | |
| JPH04108341A (en) | Method for improving blood plasma | |
| EP0726311B1 (en) | Process for preparing human activated protein c | |
| CA2150612A1 (en) | Process for producing albumin preparation | |
| WO2004014942A1 (en) | A method for preparing lipoprotein from a blood source | |
| JP2509390B2 (en) | Method for purifying collagen peptide | |
| JPS6339564A (en) | Clarification of liquid prepared from plant part | |
| SU765355A1 (en) | Method of wine stabilizing | |
| Piot et al. | Preparation of decolorized peptides from slaughter-house blood | |
| CN117126821B (en) | Separation and extraction method of bovine blood Cu-Zn superoxide dismutase | |
| JPS63132898A (en) | Separation and purification of protein | |
| JPH037556A (en) | Purification of blood plasma | |
| JPS6031479B2 (en) | Method for producing pure chondroitinase C | |
| RU1838339C (en) | Method for producing polymer composition | |
| JPS5929200B2 (en) | Manufacturing method for water-insoluble tannin preparations | |
| JPS6344600A (en) | Production of globin | |
| JPH04108342A (en) | Method for improving blood plasma | |
| CN107098966B (en) | Immunoglobulin and preparation method thereof | |
| JPS6317899A (en) | Purification of haptoglobin | |
| JPH01250331A (en) | Method for purifying glycerol | |
| SU1505428A3 (en) | Method of producing globine protein from feed blood |