JPH0775559B2 - Method for holo conversion of apoenzyme in GOT or GOT isozyme activity measurement - Google Patents
Method for holo conversion of apoenzyme in GOT or GOT isozyme activity measurementInfo
- Publication number
- JPH0775559B2 JPH0775559B2 JP21339088A JP21339088A JPH0775559B2 JP H0775559 B2 JPH0775559 B2 JP H0775559B2 JP 21339088 A JP21339088 A JP 21339088A JP 21339088 A JP21339088 A JP 21339088A JP H0775559 B2 JPH0775559 B2 JP H0775559B2
- Authority
- JP
- Japan
- Prior art keywords
- apoenzyme
- activity
- reagent
- holo
- palp
- 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
- 230000000694 effects Effects 0.000 title claims description 39
- 108010006591 Apoenzymes Proteins 0.000 title claims description 27
- 238000000034 method Methods 0.000 title claims description 22
- 238000005259 measurement Methods 0.000 title claims description 19
- 108010044467 Isoenzymes Proteins 0.000 title claims description 17
- 238000006243 chemical reaction Methods 0.000 title description 9
- 239000003153 chemical reaction reagent Substances 0.000 claims description 33
- 239000000758 substrate Substances 0.000 claims description 9
- NGVDGCNFYWLIFO-UHFFFAOYSA-N pyridoxal 5'-phosphate Chemical compound CC1=NC=C(COP(O)(O)=O)C(C=O)=C1O NGVDGCNFYWLIFO-UHFFFAOYSA-N 0.000 claims description 6
- 235000007682 pyridoxal 5'-phosphate Nutrition 0.000 claims description 3
- 239000011589 pyridoxal 5'-phosphate Substances 0.000 claims description 3
- 229960001327 pyridoxal phosphate Drugs 0.000 claims description 3
- 238000012360 testing method Methods 0.000 description 8
- 230000035484 reaction time Effects 0.000 description 7
- 210000002966 serum Anatomy 0.000 description 6
- KPGXRSRHYNQIFN-UHFFFAOYSA-N 2-oxoglutaric acid Chemical compound OC(=O)CCC(=O)C(O)=O KPGXRSRHYNQIFN-UHFFFAOYSA-N 0.000 description 4
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 4
- 229960005261 aspartic acid Drugs 0.000 description 4
- 102000003855 L-lactate dehydrogenase Human genes 0.000 description 3
- 108700023483 L-lactate dehydrogenases Proteins 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 235000003704 aspartic acid Nutrition 0.000 description 3
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 3
- 239000007983 Tris buffer Substances 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 2
- 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 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- RBCOYOYDYNXAFA-UHFFFAOYSA-L (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl phosphate Chemical compound CC1=NC=C(COP([O-])([O-])=O)C(C)=C1O RBCOYOYDYNXAFA-UHFFFAOYSA-L 0.000 description 1
- CKLJMWTZIZZHCS-UHFFFAOYSA-N D-OH-Asp Natural products OC(=O)C(N)CC(O)=O CKLJMWTZIZZHCS-UHFFFAOYSA-N 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108010025076 Holoenzymes Proteins 0.000 description 1
- CKLJMWTZIZZHCS-UWTATZPHSA-N L-Aspartic acid Natural products OC(=O)[C@H](N)CC(O)=O CKLJMWTZIZZHCS-UWTATZPHSA-N 0.000 description 1
- 102000013460 Malate Dehydrogenase Human genes 0.000 description 1
- 108010026217 Malate Dehydrogenase Proteins 0.000 description 1
- BOPGDPNILDQYTO-NNYOXOHSSA-L NADH(2-) Chemical group 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-L 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 238000010521 absorption reaction Methods 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000000872 buffer Substances 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 239000005515 coenzyme Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000002596 correlated effect Effects 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 230000002438 mitochondrial effect Effects 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000012134 supernatant fraction Substances 0.000 description 1
Landscapes
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Description
【発明の詳細な説明】 ［産業上の利用分野］ 本発明は、主として臨床検査の分野での利用を目的とし
たGOT又はGOTアイソザイムの活性測定におけるアポ酵素
のホロ化の方法に関する。DETAILED DESCRIPTION OF THE INVENTION [Industrial field of use] The present invention relates to a method for holating apoenzyme in the measurement of GOT or GOT isozyme activity mainly for use in the field of clinical examination.
［従来の技術］ GOT（glutamic oxaloacetic transminase:グルタミン酸
オキザロ酢酸トランスアミナーゼ）は、日常の臨床検査
で最も良く知られた検査項目の一つである。[Prior Art] GOT (glutamic oxaloacetic transminase) is one of the most well-known test items in daily clinical tests.
GOTにはミトコンドリア分画に存在するアイソザイム
（以下ｍ−GOTと略す。）と、細胞上清分画に存在する
アイソザイム（以下Ｓ−GOTと略す。）という局在性を
異にする二つのアイソザイムが知られており、これらの
分別定量は病態の解析に有用であるとされている。GOT has two isozymes having different localizations: an isozyme present in mitochondrial fraction (hereinafter abbreviated as m-GOT) and an isozyme present in cell supernatant fraction (hereinafter abbreviated as S-GOT). Are known, and it is said that the fractional quantification of these is useful for analysis of pathological conditions.
GOTはいわゆるビタミンB6酵素で、その補酵素はピリド
キサルリン酸（以下PALPと略す）である。一般に我が国
において行なわれていたGOT活性測定法では、試薬中にP
ALPを加えない場合が多く、このためすでにPALPと結合
しているGOTのホロ酵素のみが測定され、アポ酵素は測
定されないことになる。しかし、1976年のIFCCの勧告以
来、我が国でも試薬中にPALPを加えることによるアポ酵
素のホル化が注目され始めた。GOT is a so-called vitamin B 6 enzyme, and its coenzyme is pyridoxal phosphate (hereinafter abbreviated as PALP). In the GOT activity assay generally performed in Japan, P
In many cases, ALP is not added, so that only the GOT holoenzyme already bound to PALP is measured, and the apoenzyme is not measured. However, since the recommendation of IFCC in 1976, the forlation of apoenzyme by adding PALP in the reagent has started to be noticed in Japan.
従来、GOTの活性測定におけるアポ酵素のホロ化の方法
には、試料の血清にPALPを直接添加することによりホロ
化する方法と、試薬中にPALPを加えてから試料と反応さ
せる方法がある。Conventionally, as a method for holo-forming an apoenzyme in the measurement of GOT activity, there are a method for holo-forming by directly adding PALP to the serum of a sample and a method for adding PALP in a reagent and then reacting with the sample.
［発明が解決しようとする課題］ しかし、試料の血清にPALPを直接添加する方法は、試料
ごとに行う操作が煩雑で手間がかかる問題がある。更に
血清アルブミンなどがアポ酵素のホロ化を阻害するた
め、PALPはある程度以上の濃度が必要とされ、通常約30
μＭ以上を添加する。しかしながらPALPはGOT活性の測
定波長である340nmに大きな吸収を有するので、このよ
うな高濃度ではしばしばブランク値の上昇による測定へ
の影響が問題となる。[Problems to be Solved by the Invention] However, the method of directly adding PALP to the serum of a sample has a problem that the operation performed for each sample is complicated and time-consuming. Furthermore, since serum albumin inhibits the apoenzyme holo-formation, PALP is required to have a certain concentration or more, and is usually about 30
Add μM or more. However, since PALP has a large absorption at 340 nm, which is the measurement wavelength of GOT activity, the influence of the increase of the blank value on the measurement often becomes a problem at such a high concentration.
また試薬中にPALPを加えておく方法は操作が簡易である
が、PALPの濃度を上述より更に高くする必要があり、通
常約100μＭに達する。このためブランク値の上昇は更
に顕著で、測定に著しく影響すると共に、反応時間も30
分間以上必要なため、日常の臨床検査では支障がある。Although the method of adding PALP to the reagent is simple in operation, the concentration of PALP needs to be higher than the above, and usually reaches about 100 μM. For this reason, the increase in the blank value is more remarkable, which significantly affects the measurement and the reaction time is 30%.
Since it takes more than a minute, daily clinical examinations are a problem.
本発明の目的は、このような従来の方法を改良し、操作
が簡易で反応時間も短く、更にブランク値の上昇が少な
く日常の臨床検査で利用しうる方法として供することに
ある。An object of the present invention is to improve such a conventional method and provide it as a method which can be used in daily clinical examinations because the operation is simple, the reaction time is short, and the blank value does not increase much.
［課題を解決するための手段］ 本発明者らは上述の目的を達成するために鋭意研究をす
すめた結果、GOT活性測定試薬の少なくとも基質成分の
存在下でPALPと試料を加えると、アポ酵素のホロ化が阻
害されることを見い出し、更に研究を重ねた結果、GOT
活性測定試薬から少なくとも基質成分を除いたものにPA
LPを加えることにより調製した試薬に試料を加えて反応
させたあと、残りの成分からなる試薬を加えて反応させ
ることにより、簡易で短時間にアポ酵素のホロ化が阻害
されることなく行うことができ、PALPの添加量も少なく
することができることがわかり、本発明を完成するに至
った。[Means for Solving the Problems] As a result of intensive studies to achieve the above-mentioned object, the present inventors have found that when PALP and a sample were added in the presence of at least a substrate component of a GOT activity measurement reagent, apoenzyme As a result of discovering that holo formation of the
PA with at least the substrate component removed from the activity assay reagent
A sample can be added to the reagent prepared by adding LP to react, and then a reagent consisting of the remaining components can be added and allowed to react, so that the apoenzyme holo-formation can be performed easily and in a short time without being hindered. It was found that the amount of PALP added could be reduced, and the present invention was completed.
すなわち、本発明の要旨は、試料、とりわけ臨床検査で
用いるような血清、血漿などの検体中のGOTの活性測定
において、アポ酵素のホロ化を行うにあたり、GOT活性
測定試薬から少なくとも基質成分を除いたものにPALPを
加えてなる試薬に試料を加え、そのあとで残りの成分か
らなる試薬を加えて反応させることを特徴とするGOTの
活性測定におけるアポ酵素のホロ化の方法である。That is, the gist of the present invention is to remove at least a substrate component from a GOT activity measuring reagent in performing the apoenzyme holo conversion in the measurement of GOT activity in a sample, particularly in a sample such as serum or plasma used in a clinical test. This is a method for the aholase of an apoenzyme in the measurement of GOT activity, which comprises adding a sample to a reagent obtained by adding PALP to the above, and then adding a reagent consisting of the remaining components and reacting.
本発明の方法に用いるGOT活性測定試薬としては、本発
明の作用を有するものならば公知のGOT活性測定試薬の
いずれもが使用できる。とりわけ、波長340nmでの吸光
度変化量を測定することを原理とする試薬が、日常の臨
床検査で自動分析装置へも容易に応用できることから好
ましい。この場合の試薬成分としては、アスパラギン
酸、２−オキソグルタル酸、リンゴ酸脱水素酵素（MD
H）、乳酸脱水素酵素（LDH）、ニコチンアミド・アデニ
ン・ジヌクレオチド還元型（NADH）および緩衝剤などが
あるが。このうち、アスパラギン酸,2−オキソグルタル
酸が基質成分となり得る。As the GOT activity measuring reagent used in the method of the present invention, any known GOT activity measuring reagent can be used as long as it has the action of the present invention. In particular, a reagent based on the principle of measuring the amount of change in absorbance at a wavelength of 340 nm is preferable because it can be easily applied to an automatic analyzer in daily clinical tests. In this case, the reagent components include aspartic acid, 2-oxoglutarate, malate dehydrogenase (MD
H), lactate dehydrogenase (LDH), nicotinamide adenine dinucleotide reduced form (NADH) and buffer. Of these, aspartic acid and 2-oxoglutarate can be the substrate components.
本発明の方法はまた、GOTアイソザイム活性測定におけ
るアポ酵素のホロ化の方法でもある。すなわち、GOTア
イソザイム活性測定試薬から少なくとも基質成分を除い
たものにPALPを加えてなる試薬に試料を加え、そのあと
で残りの成分からなる試薬を加えて反応させることを特
徴とするGTOアイソザイム活性測定におけるアポ酵素の
ホロ化の方法である。The method of the present invention is also a method for making apoenzyme holo in measuring GOT isozyme activity. That is, the GTO isozyme activity measurement is characterized by adding a sample to a reagent obtained by adding PALP to a GOT isozyme activity measurement reagent from which at least a substrate component has been removed, and then adding a reagent consisting of the remaining components and reacting. Is a method of holo-forming the apoenzyme.
ここで用いるGOTアイソザイム活性測定試薬は、本発明
の作用を有するものならば公知のGOTアイソザイム活性
測定試薬のいずれもが使用できる。とりわけ、プロテア
ーゼ作用により特定分画のGOTアイソザイムを特異的に
阻害する方法（例えば特願昭62−75492号公報参照）を
応用した試薬を用いれば、好適である。この場合も前述
同様にアスパラギン酸、２−オキソグルタル酸が基質成
分となり得る。As the GOT isozyme activity measuring reagent used here, any known GOT isozyme activity measuring reagent can be used as long as it has the action of the present invention. In particular, it is preferable to use a reagent to which a method in which a specific fraction of GOT isozyme is specifically inhibited by a protease action (see, for example, Japanese Patent Application No. 62-75492) is applied. Also in this case, aspartic acid and 2-oxoglutaric acid can be used as the substrate component as described above.
前述のように本発明の方法ではGOT活性測定試薬又はGOT
アイソザイム活性測定試薬から少くとも基質成分を除い
たものにPALPを加えてなる試薬に試料を加える反応ステ
ップでアポ酵素のホロ化を行うことができる。このとき
PALPの濃度は総GOTおよびＳ−GOTの場合では10μＭあれ
ば十分にアポ酵素のホロ化ができ、この程度のPALPの濃
度はあまりブランク値に影響を与えない。As described above, in the method of the present invention, the GOT activity measuring reagent or GOT activity measuring reagent
The apoenzyme can be chlorinated in a reaction step in which a sample is added to a reagent in which PALP is added to an isozyme activity measuring reagent in which at least a substrate component is removed. At this time
In the case of total GOT and S-GOT, if the concentration of PALP is 10 μM, the apoenzyme can be sufficiently hololated, and this concentration of PALP does not affect the blank value so much.
更にｍ−GOTの場合はPALPの濃度は１μＭで良いため、
ブランク値に影響を与えることなくアポ酵素のホロ化が
できる。またこの反応ステップはいずれも５分以内に行
うことができる。Furthermore, in the case of m-GOT, the concentration of PALP is 1 μM, so
The apoenzyme can be hololated without affecting the blank value. Also, any of these reaction steps can be performed within 5 minutes.
次に、残りの成分からなる試薬を加えることにより、GO
T活性やGOTアイソザイム活性の測定を短時間で終結させ
ることができる。Then, by adding the reagent consisting of the remaining components, GO
Measurement of T activity and GOT isozyme activity can be terminated in a short time.
［実施例］ 以下実施例により本発明を具体的に説明するが、本発明
はこれらに限定されるものではない。[Examples] The present invention will be specifically described with reference to Examples below, but the present invention is not limited thereto.
実施例１ 試料としてヒト血清を用い、GOT活性測定におけるアポ
酵素のホロ化の反応ステップの反応時間を、PALPの濃度
をかえて種々変化させた。Example 1 Human serum was used as a sample, and the reaction time of the reaction step of the apoenzyme holo-formation in the GOT activity measurement was changed variously by changing the PALP concentration.
それには1.25mM NADH及び10μＭ又は１μM PALPを含む
0.1M Tris緩衝液（pH7.8）からなる試薬100μをと
り、これにヒト血清10μを加え、37℃で１、２、３、
５又は10分間加温した。次に、200mML−アスパラギン
酸、15mM ２−オキソグルタル酸、1.5単位/ml MDHおよ
び４単位/ml LDHを含む0.1M Tris緩衝液（pH7.8）から
なる試薬400μを加え、波長340nmにおける１分間あた
りの吸光度変化量に求めた。そして最大値を100％とし
て活性率を算出したところ第１表のような結果が得ら
れ、GOT活性測定におけるアポ酵素のホロ化の反応ステ
ップの反応時間は５分間で、PALPの濃度は10μＭで十分
であることがわかった。It contains 1.25 mM NADH and 10 μM or 1 μM PALP
Take 100μ of reagent consisting of 0.1M Tris buffer (pH 7.8), add 10μ of human serum to it, and add 1, 2, 3 at 37 ℃.
Warm for 5 or 10 minutes. Next, 400 μl of a reagent consisting of 0.1 mM Tris buffer (pH 7.8) containing 200 mM L-aspartic acid, 15 mM 2-oxoglutaric acid, 1.5 units / ml MDH and 4 units / ml LDH was added, and per minute at a wavelength of 340 nm. The amount of change in absorbance was calculated. Then, when the activity rate was calculated with the maximum value as 100%, the results shown in Table 1 were obtained. The reaction time of the reaction step of the apoenzyme holo-formation in the GOT activity measurement was 5 minutes, and the concentration of PALP was 10 μM. It turned out to be enough.
実施例２ 試料として精製した人由来のｍ−GOT（900単位/L）を用
い、実施例１と同様に操作してアポ酵素のホロ化の反応
ステップの反応時間を、PALPの濃度をかえて種々変化さ
せた。なおPALPについては、0.1μＭの濃度についても
行った。 Example 2 Using purified human-derived m-GOT (900 units / L) as a sample, the same operation as in Example 1 was carried out to change the reaction time of the reaction step of the apoenzyme holo-formation and the concentration of PALP. Various changes were made. PALP was also performed at a concentration of 0.1 μM.
その結果第２表のような結果が得られ、GOTアイソザイ
ムのｍ−GOT活性測定におけるアポ酵素のホロ化の反応
ステップの反応時間は５分で、PALPの濃度は１μＭで十
分であることがわかった。As a result, the results shown in Table 2 were obtained, and it was found that the reaction time of the reaction step of the apoenzyme holo-formation in the measurement of m-GOT activity of GOT isozyme was 5 minutes, and the concentration of PALP was 1 μM. It was
実施例３ 試料としてヒト血清10例について本発明の方法を実施
し、アポ酵素をホロ化してGOT活性を測定した。それに
は、実施例１と同様の操作をアポ酵素のホロ化の反応ス
テップの反応時間を５分として行った。そして得られた
吸光度変化量をあらかじめ活性既知のGOTの検量線から
活性に換算した。 Example 3 As a sample, the method of the present invention was carried out on 10 cases of human serum, and the apoenzyme was made into a holo to measure GOT activity. For that purpose, the same operation as in Example 1 was carried out with the reaction time of the reaction step for the apoenzyme holo-formation being 5 minutes. Then, the obtained amount of change in absorbance was converted into activity from a calibration curve of GOT with known activity in advance.
一方、IFCC準拠による方法［クリニカル・ケミストリー
（Clin.Chem.）第23巻第５号、1977］によりこれらの血
清を測定し、本発明の方法と比較したところ、第３表の
ようによく相関した結果が得られた。On the other hand, when these sera were measured by a method according to IFCC [Clinical Chemistry (Clin. Chem.) Vol. 23, No. 5, 1977] and compared with the method of the present invention, they were well correlated as shown in Table 3. The result was obtained.
［発明の効果］ 臨床検査においてGOTの活性測定は欠くことのできない
項目の一つであるが、近年ではそのアイソザイムである
ｍ−GOTとＳ−GOTと共にアポ酵素をホロ化して測定する
ことの臨床的意義が明らかにされつつあり、注目される
ようになった。 [Effects of the Invention] Although GOT activity measurement is one of the essential items in clinical tests, in recent years, it has been a clinical practice to measure apoenzyme together with its isozymes m-GOT and S-GOT. Its significance has been revealed, and it has come to the fore.
また一方では、臨床検査は自動化がすすみ、自動分析装
置の使用頻度が高まっている。このような背景のもと、
GOT又はGOTアイソザイム活性測定におけるアポ酵素のホ
ロ化の方法も日常の臨床検査に支障なく適用できること
が重要である。この点に関して本発明の方法は、試料ご
とにPALPを添加するような煩雑さがなく簡易に操作でき
ると共に、短時間で反応させることができ、更にPALPの
濃度が低いためブランクの上昇の心配もなく、日常の臨
床検査で有用なものとして使用できるという効果があ
る。On the other hand, clinical tests are becoming more automated, and the use of automatic analyzers is increasing. Against this background,
It is important that the method for making the apoenzyme holo in GOT or GOT isozyme activity measurement can also be applied to daily clinical tests without any problems. With respect to this point, the method of the present invention can be easily operated without the complexity of adding PALP for each sample, and can be reacted in a short time, and there is a concern that the blank will rise due to the low concentration of PALP. Instead, it has the effect that it can be used as a useful one in daily clinical tests.
Claims (2)
素のホロ化を行うにあたり、GOT活性測定試薬から少な
くとも基質成分を除いたものにピリドキサルリン酸を加
えてなる試薬に試料を加え、そのあとで残りの成分から
なる試薬を加えて反応させることを特徴とするGOTの活
性測定におけるアポ酵素のホロ化の方法。1. When measuring the activity of GOT in a sample, the sample is added to a reagent obtained by adding pyridoxal phosphate to a GOT activity measuring reagent from which at least a substrate component has been removed, in the case of performing aholization of an apoenzyme. A method for holating an apoenzyme in GOT activity measurement, which comprises reacting with a reagent comprising the remaining components.
いて、アポ酵素のホロ化を行うにあたり、GOT活性測定
試薬から少なくとも基質成分を除いたものにピリドキサ
ルリン酸を加えてなる試薬に試料を加え、そのあとで残
りの成分からなる試薬を加えて反応させることを特徴と
するGOTの活性測定におけるアポ酵素のホロ化の方法。2. When measuring the activity of a GOT isozyme in a sample, the sample is added to a reagent obtained by adding pyridoxal phosphate to a GOT activity measuring reagent from which at least a substrate component has been removed, in order to perform the apoenzyme holo-formation. A method for making apoenzyme holo in GOT activity measurement, which comprises reacting with a reagent comprising the remaining components afterwards.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP21339088A JPH0775559B2 (en) | 1988-08-24 | 1988-08-24 | Method for holo conversion of apoenzyme in GOT or GOT isozyme activity measurement |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP21339088A JPH0775559B2 (en) | 1988-08-24 | 1988-08-24 | Method for holo conversion of apoenzyme in GOT or GOT isozyme activity measurement |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH0260600A JPH0260600A (en) | 1990-03-01 |
| JPH0775559B2 true JPH0775559B2 (en) | 1995-08-16 |
Family
ID=16638408
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP21339088A Expired - Lifetime JPH0775559B2 (en) | 1988-08-24 | 1988-08-24 | Method for holo conversion of apoenzyme in GOT or GOT isozyme activity measurement |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH0775559B2 (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN117192117B (en) * | 2023-09-12 | 2025-02-18 | 浙江伊利康生物技术有限公司 | Aspartic acid aminotransferase mitochondrial isozyme detection kit and preparation method thereof |
-
1988
- 1988-08-24 JP JP21339088A patent/JPH0775559B2/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| JPH0260600A (en) | 1990-03-01 |
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