JPH07110231B2 - Stabilization of acetate kinase - Google Patents
Stabilization of acetate kinaseInfo
- Publication number
- JPH07110231B2 JPH07110231B2 JP60269182A JP26918285A JPH07110231B2 JP H07110231 B2 JPH07110231 B2 JP H07110231B2 JP 60269182 A JP60269182 A JP 60269182A JP 26918285 A JP26918285 A JP 26918285A JP H07110231 B2 JPH07110231 B2 JP H07110231B2
- Authority
- JP
- Japan
- Prior art keywords
- freeze
- acetate kinase
- present
- composition
- enzyme
- 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.)
- Expired - Lifetime
Links
- 108010092060 Acetate kinase Proteins 0.000 title claims description 9
- 230000006641 stabilisation Effects 0.000 title description 2
- 238000011105 stabilization Methods 0.000 title description 2
- 238000000034 method Methods 0.000 claims description 11
- -1 thiol compound Chemical class 0.000 claims description 11
- 230000000087 stabilizing effect Effects 0.000 claims description 7
- 102000001253 Protein Kinase Human genes 0.000 claims description 3
- 239000000203 mixture Substances 0.000 description 16
- 230000000694 effects Effects 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 9
- 108090000790 Enzymes Proteins 0.000 description 9
- 229940088598 enzyme Drugs 0.000 description 9
- ZKHQWZAMYRWXGA-UHFFFAOYSA-N Adenosine triphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)C(O)C1O ZKHQWZAMYRWXGA-UHFFFAOYSA-N 0.000 description 7
- 238000004108 freeze drying Methods 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- PWKSKIMOESPYIA-BYPYZUCNSA-N L-N-acetyl-Cysteine Chemical compound CC(=O)N[C@@H](CS)C(O)=O PWKSKIMOESPYIA-BYPYZUCNSA-N 0.000 description 5
- DTBNBXWJWCWCIK-UHFFFAOYSA-N Phosphoenolpyruvic acid Natural products OC(=O)C(=C)OP(O)(O)=O DTBNBXWJWCWCIK-UHFFFAOYSA-N 0.000 description 5
- 229960004308 acetylcysteine Drugs 0.000 description 5
- 239000003153 chemical reaction reagent Substances 0.000 description 5
- 150000001875 compounds Chemical class 0.000 description 5
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 5
- BOPGDPNILDQYTO-NNYOXOHSSA-N nicotinamide-adenine dinucleotide Chemical compound C1=CCC(C(=O)N)=CN1[C@H]1[C@H](O)[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OC[C@@H]2[C@H]([C@@H](O)[C@@H](O2)N2C3=NC=NC(N)=C3N=C2)O)O1 BOPGDPNILDQYTO-NNYOXOHSSA-N 0.000 description 5
- 239000000243 solution Substances 0.000 description 5
- 239000011550 stock solution Substances 0.000 description 5
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- UNXHWFMMPAWVPI-UHFFFAOYSA-N Erythritol Natural products OCC(O)C(O)CO UNXHWFMMPAWVPI-UHFFFAOYSA-N 0.000 description 2
- 241000193385 Geobacillus stearothermophilus Species 0.000 description 2
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000006172 buffering agent Substances 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 239000001103 potassium chloride Substances 0.000 description 2
- 235000011164 potassium chloride Nutrition 0.000 description 2
- JDIIGWSSTNUWGK-UHFFFAOYSA-N 1h-imidazol-3-ium;chloride Chemical compound [Cl-].[NH2+]1C=CN=C1 JDIIGWSSTNUWGK-UHFFFAOYSA-N 0.000 description 1
- HTMWOUBCEZXSHN-BTJKTKAUSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;(z)-but-2-enedioic acid Chemical compound OCC(N)(CO)CO.OC(=O)\C=C/C(O)=O HTMWOUBCEZXSHN-BTJKTKAUSA-N 0.000 description 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- XTWYTFMLZFPYCI-KQYNXXCUSA-N 5'-adenylphosphoric acid Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O XTWYTFMLZFPYCI-KQYNXXCUSA-N 0.000 description 1
- ZKHQWZAMYRWXGA-KQYNXXCUSA-J ATP(4-) Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O ZKHQWZAMYRWXGA-KQYNXXCUSA-J 0.000 description 1
- XTWYTFMLZFPYCI-UHFFFAOYSA-N Adenosine diphosphate Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(O)=O)C(O)C1O XTWYTFMLZFPYCI-UHFFFAOYSA-N 0.000 description 1
- 102000003914 Cholinesterases Human genes 0.000 description 1
- 108090000322 Cholinesterases Proteins 0.000 description 1
- UNXHWFMMPAWVPI-QWWZWVQMSA-N D-threitol Chemical class OC[C@@H](O)[C@H](O)CO UNXHWFMMPAWVPI-QWWZWVQMSA-N 0.000 description 1
- 239000004386 Erythritol Substances 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- 102000003855 L-lactate dehydrogenase Human genes 0.000 description 1
- 108700023483 L-lactate dehydrogenases Proteins 0.000 description 1
- 102000013009 Pyruvate Kinase Human genes 0.000 description 1
- 108020005115 Pyruvate Kinase Proteins 0.000 description 1
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 150000001356 alkyl thiols Chemical class 0.000 description 1
- 229940048961 cholinesterase Drugs 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- VHJLVAABSRFDPM-ZXZARUISSA-N dithioerythritol Chemical compound SC[C@H](O)[C@H](O)CS VHJLVAABSRFDPM-ZXZARUISSA-N 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- UNXHWFMMPAWVPI-ZXZARUISSA-N erythritol Chemical compound OC[C@H](O)[C@H](O)CO UNXHWFMMPAWVPI-ZXZARUISSA-N 0.000 description 1
- 229940009714 erythritol Drugs 0.000 description 1
- 235000019414 erythritol Nutrition 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 101150026107 ldh1 gene Proteins 0.000 description 1
- 101150041530 ldha gene Proteins 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 229950006238 nadide Drugs 0.000 description 1
- 239000007800 oxidant agent Substances 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 229930029653 phosphoenolpyruvate Natural products 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000001632 sodium acetate Substances 0.000 description 1
- 235000017281 sodium acetate Nutrition 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Enzymes And Modification Thereof (AREA)
Description
【発明の詳細な説明】 〔産業上の利用分野〕 本発明は酢酸キナーゼの安定化法に関するものである。TECHNICAL FIELD The present invention relates to a method for stabilizing acetate kinase.
酢酸キナーゼ（以下AKと略）は以下の反応 を触媒する酵素で、アデノシン三リン酸（以下ATPと
略）の再生産用酵素として、また診断等の測定用試薬の
酵素として注目、利用されている。例えば被検試料中の
酢酸を測定するための試薬や診断用試薬として以下の反
応 によって誘導された酢酸に前記反応式と同様にAKとATP
を作用させ、生成したアデノシンニリン酸を公知の手段
により測定することによるコリンエステラーゼの測定用
試薬等に応用され、その重要性がますます増加してい
る。Acetate kinase (hereinafter abbreviated as AK) is the following reaction It is an enzyme that catalyzes ATP, and has been attracting attention and used as an enzyme for reproducing adenosine triphosphate (hereinafter abbreviated as ATP) and as an enzyme for measuring reagents for diagnosis and the like. For example, the following reactions as reagents for measuring acetic acid in test samples and diagnostic reagents Acetic acid induced by AK and ATP
Is applied to a reagent for measuring cholinesterase by measuring the generated adenosine diphosphate by a known method, and its importance is increasing more and more.
B.stearothermophilus及びE.coli等が知られている。特
にB.stearothermophilus等の好熱菌より分離精製された
AKは、耐熱酵素でもありその性質は非常に良好で熱安定
性も65℃まで保証されている。しかし多くのAKは診断用
試薬としてのAK含有組成物を形成した場合に安定性に欠
け、とりわけ凍結乾燥等を行った場合その安定性が更に
損われてしまうことが判明し、製品化への障害となって
いた。B. stearothermophilus and E. coli are known. Especially isolated and purified from thermophiles such as B. stearothermophilus
AK is also a thermostable enzyme, its properties are very good, and its thermal stability is guaranteed up to 65 ° C. However, it was found that many AKs lack stability when formed into a composition containing AK as a diagnostic reagent, and the stability is further impaired especially when freeze-dried, etc. It was an obstacle.
本発明者等は上記に鑑み、AKを安定化する方法および安
定なAK組成物を求めるべく鋭意検討した結果、安定剤と
してSH基を持つ化合物、特に低分子チオール化合物を見
出し、本発明に到達した。In view of the above, the present inventors have conducted extensive studies to find a method for stabilizing AK and a stable AK composition, as a result, found a compound having an SH group as a stabilizer, particularly a low molecular weight thiol compound, and arrived at the present invention. did.
すなわち、本発明は酢酸キナーゼに低分子チオール化合
物を添加することを特徴とする酢酸キナーゼの安定化法
である。That is, the present invention is a method for stabilizing acetate kinase, which comprises adding a low molecular weight thiol compound to acetate kinase.
本発明において使用できるSH基含有化合物としては、Ｎ
−アセチルシステイン、システイン、グルタチオンなど
のシステイン含有ジ−若しくはトリ−ペプチド、ジチオ
スレイトール若しくはジチオエリスリトールなどのモノ
−若しくはジ−SH置換のスレイトール若しくはエリスリ
トール、又はメルカプトエタノールなどの低級アルキル
チオールなどの分子量310以下の低分子チオール化合物
で、これらの１種または２種以上が使用できる。好まし
くは安定性の点からＮ−アセチルシステインである。緩
衝剤としては、通常のものが使用でき、該水性組成物の
pHは10を越えるとチオール化合物の安定性が悪くなり、
６未満では系内の酵素を害するので通常６〜10とするこ
とが好ましい。Examples of the SH group-containing compound that can be used in the present invention include N
-Acetyl-cysteine, cysteine, cysteine-containing di- or tri-peptides such as glutathione, mono- or di-SH substituted threitol or erythritol such as dithiothreitol or dithioerythritol, or molecular weight 310 such as lower alkyl thiol such as mercaptoethanol. The following low molecular weight thiol compounds may be used alone or in combination of two or more. From the viewpoint of stability, N-acetyl cysteine is preferable. As the buffering agent, a usual one can be used, and the buffering agent of the aqueous composition
If the pH exceeds 10, the stability of the thiol compound will deteriorate,
If it is less than 6, the enzyme in the system is damaged, so it is usually preferable to set it to 6 to 10.
また低分子チオール化合物の使用濃度は安定化効果の点
から1mM以上であるが好ましくは10mM以上である。本発
明のAK含有製剤には必要に応じて他の成分を加えること
ができる。尚、低分子チオール化合物を酸化する強酸化
剤は除かれる。The concentration of the low molecular weight thiol compound used is 1 mM or more, preferably 10 mM or more, from the viewpoint of stabilizing effect. Other components can be added to the AK-containing preparation of the present invention as necessary. The strong oxidant that oxidizes the low molecular weight thiol compound is excluded.
本発明のAKを含有する組成物は、水性組成物として、ま
たは凍結乾燥組成物として、どちらの形態でも支障なく
使用することができる。AKを含有する水性組成物は本願
発明によって長期にわたって使用することができるよう
になり、本願発明の優位性が認められている。また、凍
結乾燥組成物は、AK含有水性組成物を通常の方法によっ
て凍結乾燥することにより得ることができるが、本願発
明のAKの安定化法により、凍結乾燥工程での酵素の失活
といった問題も発生せず、しかも、得られた凍結乾燥組
成物としてのAKの安定性も著しく高い。水性組成物であ
る場合にもAKの安定性も著しく高められている。The composition containing the AK of the present invention can be used as an aqueous composition or as a freeze-dried composition in either form without any trouble. According to the present invention, an aqueous composition containing AK can be used for a long period of time, and the superiority of the present invention is recognized. Further, the freeze-dried composition can be obtained by freeze-drying an AK-containing aqueous composition by a usual method, but the stabilization method of AK of the present invention causes a problem such as inactivation of an enzyme in the freeze-drying step. And the stability of AK as a freeze-dried composition obtained is extremely high. The stability of AK is remarkably enhanced even when it is an aqueous composition.
次にAKの酵素活性測定は次の方法によった。Next, the enzyme activity of AK was measured by the following method.
イミダゾール−塩酸緩衝液（pH7.2） 71.35 mM ATP 12.5 mM PEP 4.25 mM 塩化マグネシウム25 mM NADH 0.325 mM 塩化カリウム 93.75 mM PK 12.5 単位/ml LDH 13.75単位/ml （ただしPEPは、ホスホエノールピルビン酸、NADHは還
元型ニコチンアミドアデニンジヌクレオチド、PKはピル
ビン酸キナーゼ、及びLDHは乳酸脱水素酵素の略であ
る。） 上記濃度の反応液2.0mlに20μのAK酵素溶液を加え30
℃で５分間予加温した後、2M酢酸ナトリウム溶液を0.5m
l加え、反応を開始し340nmの吸光度を１分目から１分間
測定する。Imidazole-HCl buffer (pH7.2) 71.35 mM ATP 12.5 mM PEP 4.25 mM Magnesium chloride 25 mM NADH 0.325 mM Potassium chloride 93.75 mM PK 12.5 units / ml LDH 13.75 units / ml (However, PEP is phosphoenolpyruvate, NADH Is a reduced form of nicotinamide adenine dinucleotide, PK is an abbreviation for pyruvate kinase, and LDH is an abbreviation for lactate dehydrogenase.) Add 20μ of AK enzyme solution to 2.0 ml of the above reaction solution.
After preheating at 5 ℃ for 5 minutes, add 2M sodium acetate solution to 0.5m
Then, the reaction is started and the absorbance at 340 nm is measured for 1 minute from the 1st minute.
ΔE:1分間の吸光度変化 〔実施例〕 以下、本発明を実施例により更に具体的に説明する。 ΔE: Change in absorbance for 1 minute [Example] Hereinafter, the present invention will be described in more detail with reference to Examples.
実施例1. トリス（ヒドロキシメチル）アミノメタン−マレイン酸
（pH9.0） 100 mM 硫酸マグネシウム12.5 mM 塩化カリウム 31.25 mM ATP 6.25 mM PEP 1.25 mM NADH 0.325 mM AK 37.5 u/ml PK 12.5 u/ml LDH 6.25u/ml 上記の溶液に低分子チオール化合物の各添加剤を表１に
示す濃度で加え、25℃で４日間保存した結果を表１に示
す。但し保存開始時のAK活性を100％とした。表１から
明らかな如く溶液組成物において安定化効果が認められ
た。Example 1. Tris (hydroxymethyl) aminomethane-maleic acid (pH 9.0) 100 mM magnesium sulfate 12.5 mM potassium chloride 31.25 mM ATP 6.25 mM PEP 1.25 mM NADH 0.325 mM AK 37.5 u / ml PK 12.5 u / ml LDH 6.25 u / ml Each additive of the low molecular weight thiol compound was added to the above solution at the concentration shown in Table 1, and the results of storing at 25 ° C for 4 days are shown in Table 1. However, the AK activity at the start of storage was set to 100%. As is clear from Table 1, the stabilizing effect was recognized in the solution composition.
実施例2. AK ２×104単位 PK １×104単位 LDH １×103単位 ATP 1 ｇ PEP 0.05g NADH 0.14g 上記各成分をトリス−塩酸緩衝液（pH8.0）25mlに溶解
する。さらに低分子チオール化合物その他の添加剤を加
えた凍結乾燥原液を調製し凍結乾燥を行った。凍結乾燥
前後のAK活性の安定性を検討し表２に示す。但し凍結乾
燥前の原液の酵素活性を100％とした。表−２から明ら
かな如く無添加と比較しSH化合物によりAKは大きく安定
化された。 Example 2. AK 2 × 10 4 units PK 1 × 10 4 units LDH 1 × 10 3 units ATP 1 g PEP 0.05 g NADH 0.14 g The above components are dissolved in 25 ml Tris-HCl buffer (pH 8.0). Furthermore, a freeze-dried stock solution containing a low-molecular thiol compound and other additives was prepared and freeze-dried. The stability of AK activity before and after freeze-drying was examined and shown in Table 2. However, the enzyme activity of the stock solution before freeze-drying was set to 100%. As is clear from Table 2, the AK was greatly stabilized by the SH compound as compared with the case of no addition.
実施例3. 実施例２にて本発明の方法により調製された凍結乾燥品
を37℃にて１ケ月保存した結果を表３に示す。ただし凍
結乾燥直後のAK活性を100％とした。表３から明らかな
如く無添加では大きく失活しているがSH化合物を添加し
た場合は失活の度合は非常に小さかった。 Example 3. The results of storing the freeze-dried product prepared by the method of the present invention in Example 2 at 37 ° C. for 1 month are shown in Table 3. However, the AK activity immediately after freeze-drying was set to 100%. As is clear from Table 3, when the compound was not added, the activity was largely deactivated, but when the SH compound was added, the degree of deactivation was very small.
実施例4. 実施例２の原液組成の低分子チオール化合物（Ｎ−アセ
チルシステイン）の濃度を変化させて凍結乾燥原液を調
製し、凍結乾燥前後のAK活性を測定した。結果は第１図
に表示した。第１図のグラフから明らかな如くＮ−アセ
チルシステインを1mM加えることにより約85％の活性残
存が認められ、10mM以上にすることにより90％以上の活
性残存が認められる。 Example 4. Freeze-dried stock solutions were prepared by varying the concentration of the low-molecular-weight thiol compound (N-acetylcysteine) having the stock solution composition of Example 2, and the AK activity before and after freeze-drying was measured. The results are shown in Fig. 1. As is clear from the graph of FIG. 1, about 85% of residual activity was observed when 1 mM of N-acetylcysteine was added, and 90% or more of residual activity was observed when 10 mM or more was added.
以上から明らかな如く、本発明によれば従来、各種用途
の組成物として安定性に問題のあった酢酸キナーゼを安
定化する方法および安定な酢酸キナーゼ組成物を提供す
ることが可能となった。As is clear from the above, according to the present invention, it has become possible to provide a method for stabilizing an acetate kinase, which has conventionally been problematic in stability as a composition for various applications, and a stable acetate kinase composition.
第１図は本発明の方法にかかるAK含有組成物の凍結乾燥
後における、AK活性の残存の度合と、低分子チオール化
合物（Ｎ−アセチルシステイン）の濃度（凍結乾燥原液
での）との関係を示すグラフ図である。FIG. 1 shows the relationship between the residual level of AK activity and the concentration of a low molecular weight thiol compound (N-acetylcysteine) (in a freeze-dried stock solution) after freeze-drying of an AK-containing composition according to the method of the present invention. It is a graph figure which shows.
───────────────────────────────────────────────────── フロントページの続き (72)発明者 永田 和彦 京都府宇治市宇治小桜23番地 ユニチカ株 式会社中央研究所内 (72)発明者 松尾 隆明 京都府宇治市宇治小桜23番地 ユニチカ株 式会社中央研究所内 (56)参考文献 特開 昭56−99792（ＪＰ，Ａ) ─────────────────────────────────────────────────── ─── Continuation of front page (72) Inventor Kazuhiko Nagata 23 Uji Kozakura, Uji City, Kyoto Prefecture Unitika Central Research Institute (72) Inventor Takaaki Matsuo 23 Uji Kozakura, Uji City Kyoto Prefecture Unitika Stock Company Central Research In-house (56) Reference JP-A-56-99792 (JP, A)
Claims (1)
加することを特徴とする酢酸キナーゼの安定化法。1. A method for stabilizing an acetate kinase, which comprises adding a low molecular weight thiol compound to the acetate kinase.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP60269182A JPH07110231B2 (en) | 1985-11-29 | 1985-11-29 | Stabilization of acetate kinase |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP60269182A JPH07110231B2 (en) | 1985-11-29 | 1985-11-29 | Stabilization of acetate kinase |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP7087419A Division JP2551923B2 (en) | 1995-03-20 | 1995-03-20 | Acetate kinase composition |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS62130687A JPS62130687A (en) | 1987-06-12 |
| JPH07110231B2 true JPH07110231B2 (en) | 1995-11-29 |
Family
ID=17468821
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP60269182A Expired - Lifetime JPH07110231B2 (en) | 1985-11-29 | 1985-11-29 | Stabilization of acetate kinase |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH07110231B2 (en) |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6016232B2 (en) * | 1980-01-14 | 1985-04-24 | 和友 今堀 | Method for producing enzyme for reproducing adenosine triphosphate |
-
1985
- 1985-11-29 JP JP60269182A patent/JPH07110231B2/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| JPS62130687A (en) | 1987-06-12 |
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