JP2885864B2 - Determination of sialic acid - Google Patents
Determination of sialic acidInfo
- Publication number
- JP2885864B2 JP2885864B2 JP7643490A JP7643490A JP2885864B2 JP 2885864 B2 JP2885864 B2 JP 2885864B2 JP 7643490 A JP7643490 A JP 7643490A JP 7643490 A JP7643490 A JP 7643490A JP 2885864 B2 JP2885864 B2 JP 2885864B2
- Authority
- JP
- Japan
- Prior art keywords
- sialic acid
- glucose
- sample
- present
- reagent
- 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 - Fee Related
Links
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 title claims description 17
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 title claims description 16
- 238000006243 chemical reaction Methods 0.000 claims description 21
- 238000000034 method Methods 0.000 claims description 20
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 claims description 19
- 239000008103 glucose Substances 0.000 claims description 19
- 102000005548 Hexokinase Human genes 0.000 claims description 9
- 108700040460 Hexokinases Proteins 0.000 claims description 9
- 229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 claims description 8
- 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 claims description 8
- OVRNDRQMDRJTHS-OZRXBMAMSA-N N-acetyl-beta-D-mannosamine Chemical compound CC(=O)N[C@@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O OVRNDRQMDRJTHS-OZRXBMAMSA-N 0.000 claims description 7
- 102000048245 N-acetylneuraminate lyases Human genes 0.000 claims description 3
- 108700023220 N-acetylneuraminate lyases Proteins 0.000 claims description 3
- 108010006232 Neuraminidase Proteins 0.000 claims description 3
- 102000005348 Neuraminidase Human genes 0.000 claims description 3
- ZUQUTHURQVDNKF-WZPXOXCRSA-N 1-[(3S,4R,5S,6R)-3-amino-2,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl]ethanone Chemical compound C(C)(=O)C1(O)[C@@H](N)[C@@H](O)[C@H](O)[C@H](O1)CO ZUQUTHURQVDNKF-WZPXOXCRSA-N 0.000 claims 1
- 101710088194 Dehydrogenase Proteins 0.000 claims 1
- 238000004445 quantitative analysis Methods 0.000 claims 1
- 239000003153 chemical reaction reagent Substances 0.000 description 15
- 238000005259 measurement Methods 0.000 description 9
- 238000011002 quantification Methods 0.000 description 9
- LCTONWCANYUPML-UHFFFAOYSA-N Pyruvic acid Chemical compound CC(=O)C(O)=O LCTONWCANYUPML-UHFFFAOYSA-N 0.000 description 6
- LCTONWCANYUPML-UHFFFAOYSA-M Pyruvate Chemical compound CC(=O)C([O-])=O LCTONWCANYUPML-UHFFFAOYSA-M 0.000 description 5
- 229940076788 pyruvate Drugs 0.000 description 5
- AZQWKYJCGOJGHM-UHFFFAOYSA-N 1,4-benzoquinone Chemical compound O=C1C=CC(=O)C=C1 AZQWKYJCGOJGHM-UHFFFAOYSA-N 0.000 description 4
- 238000002835 absorbance Methods 0.000 description 4
- 238000006911 enzymatic reaction Methods 0.000 description 4
- SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 description 3
- 238000007796 conventional method Methods 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 239000000203 mixture Substances 0.000 description 3
- 229940107700 pyruvic acid Drugs 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- OIPPWFOQEKKFEE-UHFFFAOYSA-N orcinol Chemical compound CC1=CC(O)=CC(O)=C1 OIPPWFOQEKKFEE-UHFFFAOYSA-N 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- GHMLBKRAJCXXBS-UHFFFAOYSA-N resorcinol Chemical compound OC1=CC=CC(O)=C1 GHMLBKRAJCXXBS-UHFFFAOYSA-N 0.000 description 2
- CERZMXAJYMMUDR-QBTAGHCHSA-N 5-amino-3,5-dideoxy-D-glycero-D-galacto-non-2-ulopyranosonic acid Chemical compound N[C@@H]1[C@@H](O)CC(O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO CERZMXAJYMMUDR-QBTAGHCHSA-N 0.000 description 1
- 229930186217 Glycolipid Natural products 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102100029242 Hexokinase-2 Human genes 0.000 description 1
- 101710198385 Hexokinase-2 Proteins 0.000 description 1
- 101001123859 Homo sapiens Sialidase-1 Proteins 0.000 description 1
- 108010081916 N-acetylhexosamine oxidase Proteins 0.000 description 1
- 108010042687 Pyruvate Oxidase Proteins 0.000 description 1
- 102100028760 Sialidase-1 Human genes 0.000 description 1
- 208000038016 acute inflammation Diseases 0.000 description 1
- 230000006022 acute inflammation Effects 0.000 description 1
- TTWYZDPBDWHJOR-IDIVVRGQSA-L adenosine triphosphate disodium Chemical compound [Na+].[Na+].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 TTWYZDPBDWHJOR-IDIVVRGQSA-L 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 239000003638 chemical reducing agent Substances 0.000 description 1
- 238000004737 colorimetric analysis Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- CERZMXAJYMMUDR-UHFFFAOYSA-N neuraminic acid Natural products NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO CERZMXAJYMMUDR-UHFFFAOYSA-N 0.000 description 1
- 210000002381 plasma Anatomy 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- RMJPDRUNCDRUQC-MCDZGGTQSA-M sodium;[[[(2r,3s,4r,5r)-5-(6-aminopurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-hydroxyphosphoryl] hydrogen phosphate Chemical compound [Na+].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 RMJPDRUNCDRUQC-MCDZGGTQSA-M 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 210000002700 urine Anatomy 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、臨床検査の分野で利用することを目的とす
るシアル酸の定量法に関する。[Detailed description of the invention] [Industrial application field] The present invention relates to a method for quantifying sialic acid for use in the field of clinical examination.
［従来の技術］ シアル酸は、糖蛋白質および糖脂質の構成成分である
ノイラミン酸およびその誘導体の総称であり、人体にお
いてはほとんどＮ−アセチルノイラミン酸として存在し
ている。[Conventional Technology] Sialic acid is a general term for neuraminic acid and its derivatives, which are constituents of glycoproteins and glycolipids, and is almost present in the human body as N-acetylneuraminic acid.
臨床的には、種々の疾患、とりわけ悪性腫瘍や急性炎
症において血清などの試料中にシアル酸レベルの上昇が
見られるので、シアル酸の定量は、そのような疾患の診
断、経過および予後の観察に有用である。Clinically, elevated levels of sialic acid are found in samples such as serum in various diseases, especially malignant tumors and acute inflammation, so sialic acid quantification can be used to monitor the diagnosis, course and prognosis of such diseases Useful for
シアル酸の定量は、古くはエールリッヒ反応、オルシ
ノール反応、レゾルシノール反応、チオバルビツール反
応のような化学反応を原理とする比色法によって行なわ
れた。しかし、このような方法は操作が繁雑であり、反
応特異性も不充分であることから、酵素法が主流となっ
ている。In the past, sialic acid was quantified by a colorimetric method based on chemical reactions such as the Ehrlich reaction, the orcinol reaction, the resorcinol reaction, and the thiobarbitur reaction. However, such a method is complicated, and the reaction specificity is insufficient. Therefore, the enzymatic method is mainly used.
酵素法においては、下記のようにシアル酸にノイラミ
ニダーゼおよびＮ−アセチルノイラミン酸アルドラーゼ
を反応させると、ピルビン酸およびＮ−アセチルマンノ
サミンが生成するが、そのいずれかを測定することによ
ってシアル酸を定量することができる。In the enzymatic method, a reaction of sialic acid with neuraminidase and N-acetylneuraminic acid aldolase as described below produces pyruvate and N-acetylmannosamine. Can be determined.
ピルビン酸の測定は、初速度法またはエンドポイント
法により行うことができる。 The measurement of pyruvate can be performed by the initial velocity method or the end point method.
初速度法は次の反応を用い、NADHの消費を340nmにお
ける吸光度の減少として測定する： この方法は、試料中に存在する内因性のピルビン酸の
正の影響を受け、試薬ブランクが高く、更にNADHの減少
を測定するため測定範囲が狭くなるなどの欠点を有す
る。The initial rate method uses the following reaction to measure the consumption of NADH as a decrease in absorbance at 340 nm: This method is disadvantageous in that the endogenous pyruvate present in the sample is positively affected, the reagent blank is high, and the measurement range is narrowed to measure the decrease in NADH.
エンドポイント法においては、適当なキノン色素を生
成し、その吸光度を測定する。例えば次のような反応に
より生成する色素を580nmにおいて測定し得る： このエンドポイント法は内因性ピルビン酸の正の影響
を受けると共に、還元性物質による妨害も問題となる。In the end point method, an appropriate quinone dye is generated and its absorbance is measured. For example, the dye formed by the following reaction can be measured at 580 nm: This end point method is positively affected by endogenous pyruvate, and is also problematic by interference with reducing substances.
シアル酸の酵素定量のためには、ピルビン酸の代わり
にＮ−アセチルマンノサミンを測定することも有意義で
ある。For the enzyme quantification of sialic acid, it is also significant to measure N-acetylmannosamine instead of pyruvic acid.
特開昭60-184399号に開示されたNANAの酵素的定量方
法においては、アシルグルコサミン−２−エピメラーゼ
およびＮ−アセチルヘキソサミンオキシダーゼを作用さ
せてＮ−アセチルマンノサミンを測定している。この方
法は内因性ピルビン酸の影響は受けないが、還元性物質
および共役反応による妨害が大きい。In the enzymatic quantification method of NANA disclosed in JP-A-60-184399, N-acetylmannosamine is measured by the action of acylglucosamine-2-epimerase and N-acetylhexosamine oxidase. Although this method is not affected by endogenous pyruvate, it is significantly hindered by reducing substances and conjugation reactions.
特開昭63-148998号および特開昭63-148999号に開示さ
れたNANAおよびＮ−アセチルマンノサミンの定量は、次
式の酵素反応に基づいている： この反応は、内因性ピルビン酸や還元性物質による妨
害を受けないこと、NADH生成反応であるため吸光度の増
加を測定すればよいため、NADHの減少を測定する場合に
比らべ測定範囲が広くなるなど利点が多い。The quantification of NANA and N-acetylmannosamine disclosed in JP-A-63-148998 and JP-A-63-148999 is based on an enzymatic reaction of the following formula: This reaction is not hindered by endogenous pyruvic acid or reducing substances, and since it is an NADH generation reaction, it is sufficient to measure the increase in absorbance, so the measurement range is wider than when measuring the decrease in NADH. There are many advantages.
しかし、本発明者らがN-AMDHの基質特異性を検討した
ところ、この酵素はグルコースに対しても若干反応する
ことを見出した。However, when the present inventors examined the substrate specificity of N-AMDH, they found that this enzyme also slightly reacted with glucose.
血液、血清、血漿、尿などの検体は、それが健常人の
ものであっても内因性のグルコースを含有しており、特
に糖尿病のような疾患があればその含量も多い。従っ
て、前記のようなN-AMDHを用いる定量においては、試料
中のグルコースが存在すれば、その含有量に応じて測定
値が高くなってしまう。Specimens such as blood, serum, plasma, urine and the like contain endogenous glucose even if they are from a healthy person, and if there is a disease such as diabetes, the content is high. Therefore, in the quantification using N-AMDH as described above, if glucose is present in the sample, the measured value will increase according to the content thereof.
［発明が解決しようとする課題］ 本発明の目的は、そのようなグルコースによる影響を
除去し、臨床検査においてより有用なN-AMDHを用いるシ
アル酸定量法を提供することである。[Problem to be Solved by the Invention] An object of the present invention is to provide a method for quantifying sialic acid using N-AMDH, which eliminates such an influence of glucose and is more useful in clinical tests.
［課題を解決するための手段］ 前記目的は、試料中の内因性のグルコースを除去する
反応系を加えることにより達成されることがわかった。[Means for Solving the Problems] It has been found that the object is achieved by adding a reaction system for removing endogenous glucose in a sample.
従って、本発明は、試料にノイラミニダーゼおよびNA
NA−アルドラーゼを作用させて生成するＮ−アセチルマ
ンノサミンにＮ−AMDHを作用させ、生成するNADHを測定
することによる、試料中のシアル酸の定量法であって、
試料中の内因性のグルコースを除去する反応系を存在さ
せることを特徴とする定量法に関する。Thus, the present invention provides for the use of neuraminidase and NA in a sample.
A method for quantifying sialic acid in a sample, which comprises reacting N-AMDH on N-acetylmannosamine produced by acting NA-aldolase and measuring the produced NADH,
The present invention relates to a quantification method characterized by having a reaction system for removing endogenous glucose in a sample.
グルコース除去反応系は、本発明の目的を達成できる
ものならばどのようなものでもよいが、次式に示すヘキ
ソキナーゼ（HK）の酵素反応を用いることが有利であ
る： グルコースは、N-AMDHよりもHKとの反応特異性が高
い。従って、グルコースにN-AMDHとHKとを同時に作用さ
せても、グルコースはHKと即時に反応し、HK反応系によ
り完全に消費されるので、N-AMDHによるＮ−アセチルマ
ンノサミンの測定におけるグルコースの影響を除去する
ことができる。The glucose removal reaction system can be any one that can achieve the object of the present invention, but it is advantageous to use an enzymatic reaction of hexokinase (HK) represented by the following formula: Glucose has higher reaction specificity with HK than N-AMDH. Therefore, even if N-AMDH and HK act simultaneously on glucose, glucose reacts immediately with HK and is completely consumed by the HK reaction system, so that N-AMDH can be used to measure N-acetylmannosamine. The effects of glucose can be eliminated.
HK反応系は、340nmにおける吸光度、すなわちNADHの
測定に全く影響しないことも有利な点である。It is also an advantage that the HK reaction system has no influence on the absorbance at 340 nm, ie the measurement of NADH.
［発明の効果］ N-AMDHを用いる本発明の定量法は、内因性ピルビン酸
や還元性物質による妨害を受けず、NADHの測定において
ブランク値を高くとる必要がないことなどの利点に加え
て、試料中の内因性グルコースを除去する反応系を有す
る故に、グルコースによる妨害の無い正確な定量を可能
にし、繁雑な操作を要しないことから、臨床検査におい
て自動分析にも適用できる非常に有用な方法である。[Effect of the Invention] The quantification method of the present invention using N-AMDH is not affected by endogenous pyruvic acid or a reducing substance, and has the advantages of not requiring a high blank value in the measurement of NADH. Since it has a reaction system that removes endogenous glucose in a sample, it enables accurate quantification without interference by glucose, and does not require complicated operations. Is the way.
［実施例］ 実施例１ 本発明の方法によりグルコースの影響が除去できるこ
とを示す。[Example] Example 1 It is shown that the influence of glucose can be removed by the method of the present invention.
下記組成の試薬および試料を調製した： 試薬A:ノイラミニダーゼ １単位/ml N-AMDH 10単位/ml NAD 5mM MgSO4 10mM ATP2ナトリウム 10mM および ヘキソキナーゼ ２単位/ml を含有する20mMリン酸緩衝液（pH7.5） 試薬B:ATP2ナトリウムおよびヘキソキナーゼを除いた試
薬Ａの組成 試薬C:NANA−アルドラーゼ20単位/mlを含有する100mMリ
ン酸緩衝液（pH8.5） 試料:70mg/dlシアル酸溶液に、第１表記載の量でグルコ
ースを添加したもの 試料各70μｌに試薬A3.5mlを加え、37℃で５分間加温
し、これをブランクとした。次いで試薬C1.4mlを加え、
37℃で15分間加温した後、ブランクを対照として340nm
での吸光度を測定し、予め作成した検量線よりシアル酸
濃度を求めた。Reagents and samples of the following compositions were prepared: Reagent A: Neuraminidase 1 unit / ml N-AMDH 10 units / ml NAD 5 mM MgSO 4 10 mM ATP disodium 10 mM and hexokinase 2 units / ml 20 mM phosphate buffer (pH 7. 5) Reagent B: Composition of reagent A excluding sodium ATP and hexokinase Reagent C: 100 mM phosphate buffer (pH 8.5) containing 20 units / ml of NANA-aldolase Sample: 70 mg / dl sialic acid solution A sample to which glucose was added in the amount shown in Table 1 3.5 ml of reagent A was added to 70 μl of each sample, and the mixture was heated at 37 ° C. for 5 minutes and used as a blank. Next, 1.4 ml of reagent C was added,
After heating at 37 ° C for 15 minutes, the blank was set at 340 nm as a control.
Was measured, and the sialic acid concentration was determined from a previously prepared calibration curve.
試薬Ａの代わりに試薬Ｂを用いても同様に測定を行っ
た。The same measurement was performed using reagent B instead of reagent A.
結果を第１表に示す。 The results are shown in Table 1.
本発明に従って試薬Ａを用いるとシアル酸の正確な定
量が可能であるが、試薬Ｂを用いた場合にはグルコース
により測定が妨害されることがわかる。 It can be seen that accurate quantification of sialic acid is possible using reagent A according to the present invention, but that measurement is disturbed by glucose when reagent B is used.
実施例２ ヒト血清検体10例について、実施例１に記載の方法と
従来の方法に従い日立自動分析装置を用い、シアル酸の
定量を行った。Example 2 For 10 human serum samples, sialic acid was quantified using a Hitachi automatic analyzer according to the method described in Example 1 and a conventional method.
従来法は、ピルビン酸オキシダーゼおよびHSDAを用い
るキノン色素の測定に基づくもので、市販されているシ
アル酸測定試薬「デタミナーSA」を用いて行った。The conventional method is based on the measurement of a quinone dye using pyruvate oxidase and HSDA, and was carried out using a commercially available sialic acid measurement reagent "Determiner SA".
結果を第２表に示す。 The results are shown in Table 2.
試薬Ａを用いる本発明の方法の測定値と従来法の測定
値とは相関性が高いが、試薬Ｂを用いた場合はグルコー
スの影響により高い測定値が得られる。 Although the measured value of the method of the present invention using the reagent A and the measured value of the conventional method have a high correlation, when the reagent B is used, a high measured value is obtained due to the influence of glucose.
───────────────────────────────────────────────────── フロントページの続き (58)調査した分野(Int.Cl.6，ＤＢ名) C12Q 1/00 - 3/00 ＷＰＩ（ＤＩＡＬＯＧ) ＢＩＯＳＩＳ（ＤＩＡＬＯＧ)────────────────────────────────────────────────── ─── Continued on the front page (58) Field surveyed (Int. Cl. 6 , DB name) C12Q 1/00-3/00 WPI (DIALOG) BIOSIS (DIALOG)
Claims (2)
ルノイラミン酸アルドラーゼを作用させて生成するＮ−
アセチルマンノサミンにＮ−アセチルマンノサミン脱水
素酵素を作用させ、生成するNADHを測定することによ
る、試料中のシアル酸の定量法において、試料中の内因
性のグルコースを除去する反応系を存在させることを特
徴とする定量法。The present invention relates to a method in which a sample is treated with neuraminidase and N-acetylneuraminic acid aldolase to produce N-
By reacting acetylmannosamine with N-acetylmannosamine dehydrogenase and measuring the generated NADH, in a method for quantifying sialic acid in a sample, a reaction system for removing endogenous glucose in the sample is used. A quantitative method characterized by being present.
ソキナーゼを用いる第１項記載の定量法。2. The method according to claim 1, wherein hexokinase is used as a reaction system for removing glucose.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP7643490A JP2885864B2 (en) | 1990-03-26 | 1990-03-26 | Determination of sialic acid |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP7643490A JP2885864B2 (en) | 1990-03-26 | 1990-03-26 | Determination of sialic acid |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JPH03277296A JPH03277296A (en) | 1991-12-09 |
| JP2885864B2 true JP2885864B2 (en) | 1999-04-26 |
Family
ID=13605049
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP7643490A Expired - Fee Related JP2885864B2 (en) | 1990-03-26 | 1990-03-26 | Determination of sialic acid |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JP2885864B2 (en) |
Families Citing this family (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN118995880A (en) * | 2024-09-05 | 2024-11-22 | 北京国科星联科技有限公司 | A method for detecting sialic acid |
-
1990
- 1990-03-26 JP JP7643490A patent/JP2885864B2/en not_active Expired - Fee Related
Also Published As
| Publication number | Publication date |
|---|---|
| JPH03277296A (en) | 1991-12-09 |
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