JPS6253149B2 - - Google Patents
Info
- Publication number
- JPS6253149B2 JPS6253149B2 JP56031932A JP3193281A JPS6253149B2 JP S6253149 B2 JPS6253149 B2 JP S6253149B2 JP 56031932 A JP56031932 A JP 56031932A JP 3193281 A JP3193281 A JP 3193281A JP S6253149 B2 JPS6253149 B2 JP S6253149B2
- Authority
- JP
- Japan
- Prior art keywords
- nucleotide pyrophosphatase
- nucleotide
- pyrophosphatase
- solution
- culture
- 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
Links
- 102100021969 Nucleotide pyrophosphatase Human genes 0.000 claims description 22
- 108010027581 nucleoside triphosphate pyrophosphatase Proteins 0.000 claims description 22
- 108010067588 nucleotide pyrophosphatase Proteins 0.000 claims description 22
- 241000894006 Bacteria Species 0.000 claims description 8
- 241000192023 Sarcina Species 0.000 claims description 5
- 238000004519 manufacturing process Methods 0.000 claims description 5
- 241000192041 Micrococcus Species 0.000 claims description 3
- 238000012258 culturing Methods 0.000 claims description 2
- 239000000243 solution Substances 0.000 description 9
- BAWFJGJZGIEFAR-NNYOXOHSSA-N NAD zwitterion Chemical compound NC(=O)C1=CC=C[N+]([C@H]2[C@@H]([C@H](O)[C@@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 BAWFJGJZGIEFAR-NNYOXOHSSA-N 0.000 description 8
- 229950006238 nadide Drugs 0.000 description 8
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 8
- 102000004190 Enzymes Human genes 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 239000002609 medium Substances 0.000 description 6
- 239000007788 liquid Substances 0.000 description 5
- 230000001580 bacterial effect Effects 0.000 description 4
- SRNWOUGRCWSEMX-KEOHHSTQSA-N ADP-beta-D-ribose Chemical compound C([C@H]1O[C@H]([C@@H]([C@@H]1O)O)N1C=2N=CN=C(C=2N=C1)N)OP(O)(=O)OP(O)(=O)OC[C@H]1O[C@@H](O)[C@H](O)[C@@H]1O SRNWOUGRCWSEMX-KEOHHSTQSA-N 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- VWWQXMAJTJZDQX-UYBVJOGSSA-N flavin adenine dinucleotide Chemical compound C1=NC2=C(N)N=CN=C2N1[C@@H]([C@H](O)[C@@H]1O)O[C@@H]1CO[P@](O)(=O)O[P@@](O)(=O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C2=NC(=O)NC(=O)C2=NC2=C1C=C(C)C(C)=C2 VWWQXMAJTJZDQX-UYBVJOGSSA-N 0.000 description 3
- 235000019162 flavin adenine dinucleotide Nutrition 0.000 description 3
- 239000011714 flavin adenine dinucleotide Substances 0.000 description 3
- 229940093632 flavin-adenine dinucleotide Drugs 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- PWJFNRJRHXWEPT-UHFFFAOYSA-N ADP ribose Natural products C1=NC=2C(N)=NC=NC=2N1C1OC(COP(O)(=O)OP(O)(=O)OCC(O)C(O)C(O)C=O)C(O)C1O PWJFNRJRHXWEPT-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241000218943 Brachybacterium conglomeratum Species 0.000 description 2
- 241000196324 Embryophyta Species 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 229920005654 Sephadex Polymers 0.000 description 2
- 239000012507 Sephadex™ Substances 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- LFTYTUAZOPRMMI-CFRASDGPSA-N UDP-N-acetyl-alpha-D-glucosamine Chemical compound O1[C@H](CO)[C@@H](O)[C@H](O)[C@@H](NC(=O)C)[C@H]1OP(O)(=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(NC(=O)C=C2)=O)O1 LFTYTUAZOPRMMI-CFRASDGPSA-N 0.000 description 2
- LFTYTUAZOPRMMI-UHFFFAOYSA-N UNPD164450 Natural products O1C(CO)C(O)C(O)C(NC(=O)C)C1OP(O)(=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(NC(=O)C=C2)=O)O1 LFTYTUAZOPRMMI-UHFFFAOYSA-N 0.000 description 2
- 238000002523 gelfiltration Methods 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 238000009776 industrial production Methods 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 239000002777 nucleoside Substances 0.000 description 2
- -1 nucleoside monophosphates Chemical class 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 238000011218 seed culture Methods 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- SRNWOUGRCWSEMX-UHFFFAOYSA-N Adenosine diphosphate ribose Natural products C1=NC=2C(N)=NC=NC=2N1C(C(C1O)O)OC1COP(O)(=O)OP(O)(=O)OCC1OC(O)C(O)C1O SRNWOUGRCWSEMX-UHFFFAOYSA-N 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 1
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 241000272201 Columbiformes Species 0.000 description 1
- 229910021591 Copper(I) chloride Inorganic materials 0.000 description 1
- 241000192091 Deinococcus radiodurans Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- 108010009413 Pyrophosphatases Proteins 0.000 description 1
- 102000009609 Pyrophosphatases Human genes 0.000 description 1
- 235000002595 Solanum tuberosum Nutrition 0.000 description 1
- 244000061456 Solanum tuberosum Species 0.000 description 1
- HSCJRCZFDFQWRP-JZMIEXBBSA-N UDP-alpha-D-glucose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OP(O)(=O)OP(O)(=O)OC[C@@H]1[C@@H](O)[C@@H](O)[C@H](N2C(NC(=O)C=C2)=O)O1 HSCJRCZFDFQWRP-JZMIEXBBSA-N 0.000 description 1
- HSCJRCZFDFQWRP-UHFFFAOYSA-N Uridindiphosphoglukose Natural products OC1C(O)C(O)C(CO)OC1OP(O)(=O)OP(O)(=O)OCC1C(O)C(O)C(N2C(NC(=O)C=C2)=O)O1 HSCJRCZFDFQWRP-UHFFFAOYSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- OXBLHERUFWYNTN-UHFFFAOYSA-M copper(I) chloride Chemical compound [Cu]Cl OXBLHERUFWYNTN-UHFFFAOYSA-M 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- FVTCRASFADXXNN-SCRDCRAPSA-N flavin mononucleotide Chemical compound OP(=O)(O)OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O FVTCRASFADXXNN-SCRDCRAPSA-N 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229910021645 metal ion Inorganic materials 0.000 description 1
- 238000000034 method Methods 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 235000012015 potatoes Nutrition 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- FQENQNTWSFEDLI-UHFFFAOYSA-J sodium diphosphate Chemical compound [Na+].[Na+].[Na+].[Na+].[O-]P([O-])(=O)OP([O-])([O-])=O FQENQNTWSFEDLI-UHFFFAOYSA-J 0.000 description 1
- 229940048086 sodium pyrophosphate Drugs 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 235000019818 tetrasodium diphosphate Nutrition 0.000 description 1
- 239000001577 tetrasodium phosphonato phosphate Substances 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
Landscapes
- Enzymes And Modification Thereof (AREA)
Description
【発明の詳細な説明】
本発明はヌクレオチドピロホスフアターゼを製
造する方法に関する。DETAILED DESCRIPTION OF THE INVENTION The present invention relates to a method for producing nucleotide pyrophosphatases.
更に詳細には、本発明は、ヌクレオチドピロホ
スフアターゼを菌体外に生成させ、有効に採取す
る方法に関するものである。 More specifically, the present invention relates to a method for producing nucleotide pyrophosphatase outside of bacterial cells and effectively collecting it.
一般に、ヌクレオチドピロホスフアターゼ
（3.6.1.9）は次の反応式に示される如く、FAD、
NAD、ADP−ribose、NADP、UDPG等のヌクレ
オチドを分解し、ヌクレオシドモノホスフエート
を生成させる酵素としてよく知られている。 In general, nucleotide pyrophosphatase (3.6.1.9) is FAD, as shown in the following reaction formula.
It is well known as an enzyme that degrades nucleotides such as NAD, ADP-ribose, NADP, and UDPG to produce nucleoside monophosphates.
ヌクレオチドピロホスフアターゼの給源をジヤ
ガイモ、ハトなどの動植物や多くの微生物に求め
ることはできるが、動植物からではとうてい工業
的生産はできず、また、微生物においても、その
ほとんどが菌体内に生産するために、精製が困難
であつて、工業的生産には適していなかつた。 Although sources of nucleotide pyrophosphatase can be found in plants and animals such as potatoes and pigeons, as well as in many microorganisms, industrial production from plants and animals is hardly possible, and even in microorganisms, most of it is produced within the bacterial cells. Therefore, it was difficult to purify and was not suitable for industrial production.
本発明者らは、ヌクレオチドピロホスフアター
ゼを有効に生産する菌を求めて多くの微生物を検
索したところ、ミクロコツカス属とサルシナ属に
属する菌においてヌクレオチドピロホスフアター
ゼを菌体外に生産し、工業生産的にきわめてすぐ
れた菌株があることを見出した。 The present inventors searched many microorganisms in search of bacteria that effectively produce nucleotide pyrophosphatase, and found that bacteria belonging to the genus Micrococcus and Sarcina produced nucleotide pyrophosphatase extracellularly. We have discovered that there is a strain of bacteria that has excellent industrial productivity.
本発明は、この知見より完成されたもので、ミ
クロコツカス属又はサルシナ属に属するヌクレオ
チドピロホスフアターゼ菌体外生産菌を培養し、
培養物よりヌクレオチドピロホスフアターゼを採
取することを特徴とするヌクレオチドピロホスフ
アターゼの製造法である。 The present invention was completed based on this knowledge, and involves culturing a nucleotide pyrophosphatase producing bacterium belonging to the genus Micrococcus or Sarcina in vitro.
This is a method for producing nucleotide pyrophosphatase, which is characterized by collecting nucleotide pyrophosphatase from a culture.
本発明に使用するヌクレオチドピロホスフアタ
ーゼ菌体外生産菌の例示としては、
Micrococcus conglomeratus IAM 1459
Micrococcus radiodurans IAM 12271
Sarcina albida IAM 1012
があげられる。 Examples of the nucleotide pyrophosphatase extracellular producing bacteria used in the present invention include Micrococcus conglomeratus IAM 1459 Micrococcus radiodurans IAM 12271 Sarcina albida IAM 1012.
これら使用菌は培養培地で培養される。培地と
しては菌体外に酵素を生産させるために液体培地
が用いられる。培地は炭素源、窒素源、無機塩等
適宜含有するものであれば、いかなる培地でもよ
い。 These used bacteria are cultured in a culture medium. A liquid medium is used to produce enzymes outside the bacterial cells. The medium may be any medium as long as it contains appropriate carbon sources, nitrogen sources, inorganic salts, etc.
使用菌の種培養液を培養培地に接種した後、20
〜40℃で、通気撹拌で、20〜50時間培養される。 After inoculating the culture medium with the seed culture of the bacteria used,
Incubate for 20-50 hours at ~40°C with aeration and agitation.
培養液は過もしくは遠心分離によつて菌体を
分離除去し、除菌液を得る。 The bacterial cells are separated and removed from the culture solution by filtration or centrifugation to obtain a sterilized solution.
得られた培養除菌液は、限外過膜（Ｇ−
05T）によつて濃縮し、更にSephadexG100ゲル
過、WhatmanDE−52等による精製を行うこと
によつてヌクレオチドピロホスフアターゼを精製
単離することができる。 The obtained culture sterilization solution was passed through an ultrafiltration membrane (G-
Nucleotide pyrophosphatase can be purified and isolated by concentrating with 05T) and further purifying with Sephadex G100 gel filtration, Whatman DE-52, etc.
本発明における精製ヌクレオチドピロホスフア
ターゼはこのまま分析用、生産用等に使用するこ
とができるが、必要によつては液状物を凍結乾燥
して粉末状とて単離することも可能である。 The purified nucleotide pyrophosphatase of the present invention can be used as it is for analysis, production, etc., but if necessary, it can also be isolated as a powder by freeze-drying the liquid.
次に、本発明において得られるヌクレオチドピ
ロホスフアターゼの理化学的性質を示す。 Next, the physicochemical properties of the nucleotide pyrophosphatase obtained in the present invention will be shown.
１ FAD（flavin adenine dinucleotide）、
NAD（nicotinamide adenine
dinucleotide）、
ADP−ribose（adenosine diphosphate−
ribose）、
NADP（nicotinamide adenine dinucleotide
phosphate）、
UDP−GlcNAc（uridine diphosphate Ｎ−
acetyl glucosamine）
に作用して、各ヌクレオシドモノホスフエート
を生成する。1 FAD (flavin adenine dinucleotide), NAD (nicotinamide adenine
dinucleotide), ADP−ribose(adenosine diphosphate−
ribose), NADP (nicotinamide adenine dinucleotide)
phosphate), UDP-GlcNAc (uridine diphosphate N-
acetyl glucosamine) to produce each nucleoside monophosphate.
２ AMP、ADP、ATP、NMN、FMNには作用
しない。2 Does not affect AMP, ADP, ATP, NMN, FMN.
３ 至適PHは7.0〜9.0である。3 Optimum pH is 7.0-9.0.
４ 安定PH：PH７〜９の範囲で、５℃で安定。4. Stable pH: PH7-9, stable at 5℃.
５ 温度安定性：30℃60分処理では安定。5 Temperature stability: Stable when treated at 30℃ for 60 minutes.
６ 至適温度：30℃附近にある。6 Optimum temperature: Around 30℃.
７ 金属イオンの影響：１ｍＭのZnCl2 １ｍＭのCuCl2 １ｍＭのSnCl2 １ｍＭのFeCl3 によつて阻害される。7 Effect of metal ions: Inhibited by 1mM ZnCl 2 1mM CuCl 2 1mM SnCl 2 1mM FeCl 3 .
８ 分子量：約４万（ゲル過法による）
本酵素は酵素分類3.6.1.9nucleotide
pyrophosphataseと一致するものである。8 Molecular weight: Approximately 40,000 (by gel filtration method) This enzyme is classified as enzyme 3.6.1.9nucleotide
It is consistent with pyrophosphatase.
次に本発明の実施例を示す。 Next, examples of the present invention will be shown.
なお、ヌクレオチドピロホスフアターゼの活性
測定は、270μの酵素標品にNAD（20mg／ml）
30μを加え、30℃１〜６時間反応し、該反応を
95％エタノール0.1mlを含む50ｍＭのソデイウム
ピロホスフエート（PH8.8）2.5mlにてストツプさ
せ、ついでアルコールデヒドロゲナーゼを0.1％
アルブミンを含む10ｍＭ燐酸緩衝液（PH7.5）に
て溶解し20u／mlとしたもの0.1mlを添加し、還元
型NADの340nｍでのODの減少をみることにより
求められる。対照には酵素標品の代わりにトリス
緩衝液を用いる。この場合の単位の表示は１分当
りOD340nｍの吸光度0.001の減少を1uとする。 For measuring the activity of nucleotide pyrophosphatase, add NAD (20mg/ml) to the 270μ enzyme preparation.
Add 30μ and react for 1 to 6 hours at 30°C.
Stop with 2.5 ml of 50 mM sodium pyrophosphate (PH8.8) containing 0.1 ml of 95% ethanol, then add 0.1% alcohol dehydrogenase.
It is determined by adding 0.1 ml of 20 u/ml dissolved in 10 mM phosphate buffer (PH7.5) containing albumin and observing the decrease in OD of reduced NAD at 340 nm. For controls, use Tris buffer instead of the enzyme preparation. In this case, the units are expressed as 1 u, which is a decrease of 0.001 in absorbance at OD340 nm per minute.
実施例 １
（普通ブイヨン培地）
肉エキス ３ｇ
ペプトン 10ｇ
NaCl ５ｇ
水を加えて１とする（PH7.0）
上記組成の培地100mlにSarcina
albidaIAM1012を接種し、30℃で24時間種培養
し、得られた種培養液100mlを同じ組成の培地10
に添加して30℃で40時間好気的に培養した。Example 1 (Normal bouillon medium) Meat extract 3g Peptone 10g NaCl 5g Add water to make 1 (PH7.0) Add Sarcina to 100ml of the medium with the above composition.
albidaIAM1012 was inoculated and cultured at 30°C for 24 hours, and 100ml of the resulting seed culture was added to 10ml of a medium with the same composition.
and cultured aerobically at 30°C for 40 hours.
得られた培養液を3000rpmで15分間遠心分離処
理し、次に、液をＧ−05Tで限外過濃縮し、
液510mlを得る。この液はヌクレオチドピロ
ホスフアターゼ活性0.4u／mlであつた。 The obtained culture solution was centrifuged at 3000 rpm for 15 minutes, and then the solution was ultra-superconcentrated using G-05T.
Obtain 510ml of liquid. This solution had a nucleotide pyrophosphatase activity of 0.4 u/ml.
得られた液510mlを1.2SephadexG100カラ
ムに60mlずつチヤージし、流速60ml／hrで、24
ml／tubeで分画し、フラクシヨンNo.46、47、
48、49、50、51を集め、これをＧ−05Tで限外
過濃縮し、液650mlを得る。この液はヌクレ
オチドピロホスフアターゼ活性4.5u／mlであつ
た。更に、該液中のヌクレオチドピロホスフア
ターゼをトリス緩衝液で緩衝化したワツトマン
DE−52に吸着せしめ、次いで、０〜0.5Mの食塩
水でグラジエント溶出し、活性画分を集めた。こ
の溶出液64mlのヌクレオチドピロホスフアターゼ
活性は34.8u／mlであつた。 Charge 510 ml of the obtained liquid to a 1.2 Sephadex G100 column in 60 ml portions at a flow rate of 60 ml/hr for 24 hours.
Fractionate by ml/tube, fraction No. 46, 47,
48, 49, 50, and 51 were collected and ultra-concentrated using G-05T to obtain 650 ml of liquid. This solution had a nucleotide pyrophosphatase activity of 4.5 u/ml. Furthermore, the nucleotide pyrophosphatase in the solution was buffered with a Tris buffer.
It was adsorbed onto DE-52, and then eluted with a gradient of 0 to 0.5M saline, and the active fractions were collected. The nucleotide pyrophosphatase activity of 64 ml of this eluate was 34.8 u/ml.
実施例 ２
Micrococcus conglomeratusIAM1459を用いて
実施例１と全く同様に処理し、ヌクレオチドピロ
ホスフアターゼ活性0.5u／mlの液を得た。Example 2 Micrococcus conglomeratus IAM1459 was treated in exactly the same manner as in Example 1 to obtain a solution with nucleotide pyrophosphatase activity of 0.5 u/ml.
Claims (1)
クレオチドピロホスフアターゼ菌体外生産菌を培
養し、培養物よりヌクレオチドピロホスフアター
ゼを採取することを特徴とするヌクレオチドピロ
ホスフアターゼの製造法。1. A method for producing nucleotide pyrophosphatase, which comprises culturing a nucleotide pyrophosphatase extracellular producing bacterium belonging to the genus Micrococcus or the genus Sarcina, and collecting nucleotide pyrophosphatase from the culture.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP56031932A JPS57146574A (en) | 1981-03-07 | 1981-03-07 | Preparation of nucleotide pyrophosphatase |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP56031932A JPS57146574A (en) | 1981-03-07 | 1981-03-07 | Preparation of nucleotide pyrophosphatase |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPS57146574A JPS57146574A (en) | 1982-09-10 |
| JPS6253149B2 true JPS6253149B2 (en) | 1987-11-09 |
Family
ID=12344738
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP56031932A Granted JPS57146574A (en) | 1981-03-07 | 1981-03-07 | Preparation of nucleotide pyrophosphatase |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPS57146574A (en) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2698206T3 (en) * | 2004-06-29 | 2019-02-01 | Puratos Nv | Mass comprising nucleotide pyrophosphatase inhibitor |
| US8187646B2 (en) | 2004-06-29 | 2012-05-29 | Puratos N.V. | Nucleotide pyrophosphatase inhibitor and coenzyme regenerating systems |
-
1981
- 1981-03-07 JP JP56031932A patent/JPS57146574A/en active Granted
Also Published As
| Publication number | Publication date |
|---|---|
| JPS57146574A (en) | 1982-09-10 |
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