分类目录归档：龟甲万 Kikkoman

日本kikkoman龟甲万Fructosyl-peptide Oxidase (FPOX-CE) 果糖基 – 缩氨酸氧化酶

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Fructosyl-peptide Oxidase (FPOX-CE) 果糖基 – 缩氨酸氧化酶

  • 临床检测用酶

The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.

由来 recombinant E. coli
系统名称

Fructosyl-peptide : oxygen oxidoreductase
EC编号 1.5.3
反应式

Fructosyl-L-amino acid + H2O + O2 →→→ Peptide + Glucosone + H2O2

规格

Appearance yellow lyophilizate
Activity

≧6.0 U/mg
Contaminants Catalase　≦1.0 U/U％
Stabilizer ethylenediaminetetraacetic acid (EDTA), sodium glutamate
Storage condition below -20℃ protected from light

特性

Molecular weight ca. 60kDa (gel filtration)
Structure monomer of 52 kDa (SDS-PAGE)
Isoelectric point 4.2
Michaelis constant 3.4×10-3M (fructosyl-valyl-histidine)
4.4×10-3M (fructosyl-glycine)
8.9×10-3M (Nε-fructosyl-lysine)
pH Optimum 7.5–8.0
pH Stability 6.0–9.5
Optimum temperature 35–42℃
Thermal stability below 45℃
Stability (powder form) stable at 37℃ for at least one month
Specificity fructosyl-valyl-histidine (100), fructosyl-glycine (53)
Nε-fructosyl-lysine (84)

适用类型

The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.

参考文献

Hirokawa K, Gomi K, Bakke M, Kajiyama N. (2003)
Distribution and properties of novel deglycating enzymes for fructosyl peptide in fungi.
Archives of Microbiology, 180, 227-231.

Hirokawa K, Gomi K, Kajiyama N. (2003)
Molecular cloning and expression of novel fructosyl peptide oxidases and their application for the measurement of glycated protein.
Biochem Biophys Res Commun, 311(1), 104-111.

Hirokawa K, Shimoji K, Kajiyama N. (2005)
An enzymatic method for the determination of hemoglobinA1C.
Biotechnology Letters, 27(14), 963-968.

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日本kikkoman龟甲万Fructosyl-peptide Oxidase (FPOX-CET) 果糖基 – 缩氨酸氧化酶

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Fructosyl-peptide Oxidase (FPOX-CET) 果糖基 – 缩氨酸氧化酶

  • 临床检测用酶

The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.

由来 recombinant E. coli
系统名称

Fructosyl-peptide : oxygen oxidoreductase
EC编号 1.5.3
反应式

Fructosyl-L-amino acid + H2O + O2 →→→ Peptide + Glucosone + H2O2

规格

Appearance yellow lyophilizate
Activity ≧5.0 U/mg
Contaminants Catalase　≦1.0 U/U％
Stabilizer sodium glutamate, ethylenediaminetetraacetic acid (EDTA)
Storage condition below -20℃ protected from light

特性

Molecular weight ca. 60 kDa (gel filtration)
Structure monomer of 52 kDa(SDS-PAGE)
Michaelis constant 1.5×10-3M(fructosyl-valyl-histidine)
5.0×10-3M (fructosyl-glysine)
9.0×10-3M(Nε-fructosyl-lysine)
pH Optimum 7.5–8.5
pH Stability 5.5–9.5
Optimum temperature 37–45℃
Thermal stability below 45℃
Stability (powder form) stable at -20℃ for at least 12 months
Specificity fructosyl-valyl-histidine (100), fructosyl-glycine(150)
Nε-fructosyl-L-lysine (68.6)

适用类型

The enzyme is useful for the determination of fructosyl-peptide and fructosyl-L-amino acid.

参考文献

Hirokawa K, Shimoji K, Kajiyama N. (2005)
An enzymatic method for the determination of hemoglobinA1C.
Biotechnology Letters, 27(14), 963-968.

Hirokawa K, Ichiyanagi A, Kajiyama N. (2008)
Enhancement of thermostability of fungal deglycating enzymes by directed evolution.
Applied Mcrobiology and Biotechnology, 78(5), 775-781.

Ichiyanagi A, Hirokawa K, Gomi K, Nakatsu T, Kato H, Kajiyama N. (2013)
Crystallization and preliminary crystallographic analysis of two eukaryotic fructosyl peptide oxidases.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 69(2), 130-133.

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日本kikkoman龟甲万Glucose Dehydrogenase (FADGDH-AA) 葡萄糖脱氢酶

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Glucose Dehydrogenase (FADGDH-AA) 葡萄糖脱氢酶

  • 临床检测用酶

The enzyme is useful for the determination of D-glucose in clinical analysis and self-monitoring blood glucose meters.

由来 recombinant A. sojae
系统名称

D-Glucose : acceptor 1-oxidoreductase
EC编号 1.1.5.9
反应式

D-Glucose + acceptor →→→ D-Glucono-1,5-lactone + reduced acceptor

规格

Appearance yellow lyophilizate
Activity ≧500 U/mg
Contaminants NAD glucose dehydrogenase　 ≺1.0×10-2％
Hexokinase　≺1.0×10-2 U/U%
α-Glucosidase　≺1.0×10-2 U/U%
β-Glucosidase　≺1.0×10-2 U/U%
Storage condition below -20℃ protected from light

特性

Molecular weight ca. 90 kDa (gel filtration)
Structure monomer, one mole of FAD per mole of enzyme glycoprotein
Michaelis constant 9.5×10-2M (D-glucose)
pH Optimum 7.0–7.5
pH Stability 2.5–7.5
Optimum temperature 40–50℃
Thermal stability below 50℃
Inhibitors Ag+
Specificity D-glucose (100), maltose (≺1), 
D-xylose (≺1), D-galactose (≺1) 

适用类型

The enzyme is useful for the determination of D-glucose in clinical analysis and self-monitoring blood glucose meters.

参考文献

Satake, R. et al., J Biosci Bioeng., 120, 498–503 (2015)

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日本kikkoman龟甲万Glucose Dehydrogenase (FADGDH-AB) 葡萄糖脱氢酶

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Glucose Dehydrogenase (FADGDH-AB) 葡萄糖脱氢酶

  • 临床检测用酶

The enzyme is useful for the determination of d-glucose in clinical analysis and self-monitoring blood glucose meters.

系统名称

D-Glucose : acceptor 1-oxidoreductase
EC编号 1.1.5.9
反应式

D-Glucose + acceptor →→→ D-Glucono-1,5-lactone + reduced acceptor

规格

Appearance Yellow lyophilizate
Activity ≧700 U/mg lyophilizate
Contaminant NAD Glucose Dehydrogenase　 ≺1.0×10-2％
Hexokinase　≺1.0×10-2％
α-Glucosidase　≺1.0×10-2％
β-Glucosidase　≺1.0×10-2％
Storage below -20℃ protected from light

特性

Molecular weight ca. 85 kDa (SDS-PAGE)
Structure monomer, one mole of FAD per mole of enzyme glycoprotein
Michaelis constant 2.2×10-2M (D-Glucose)
pH Optimum 7.0–7.5
pH Stability 4.5–8.0
Optimum temperature 40–50℃
Thermal stability below 45℃
Specificity D-glucose (100), Maltose (≺0.3), 
D-xylose (≺10), D-galactose (≺1.2) 
sucrose (≺0.0) 

适用类型

The enzyme is useful for the determination of D-glucose in clinical analysis and self-monitoring blood glucose meters.

参考文献

Hatada M, Loew N, Inose-Takahashi Y, Okuda-Shimazaki J, Tsugawa W, Mulchandani A, Sode K (2018)
Development of a glucose sensor employing quick and easy modification method with mediator for altering electron acceptor preference.
Bioelectrochemistry, 121, 185-190

Okuda-Shimazaki, J, Yoshida H, Sode K (2020)
FAD dependent glucose dehydrogenases – Discovery and engineering of representative glucose sensing enzymes –
Bioelectrochemistry, 132, 107414

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日本kikkoman龟甲万Glucose Dehydrogenase (FADGDH-AD) 葡萄糖脱氢酶

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Glucose Dehydrogenase (FADGDH-AD) 葡萄糖脱氢酶

  • 临床检测用酶

The enzyme is useful for the determination of blood glucose and for continuous glucose monitoring (CGM) sensor.

由来 recombinant Aspergillus sojae
系统名称

D-Glucose : acceptor 1-oxidoreductase
EC编号 1.1.5.9
反应式

D-Glucose + acceptor →→→ D-Glucono-1,5-lactone + reduced acceptor

规格

Appearance yellow to brown lyophilizate
Activity ≧700 U/mg
Contaminants NAD glucose dehydrogenase　 <0.01 U/U%
Hexokinase　 <0.01 U/U%
α-glucosidase　 <0.01 U/U%
β-glucosidase　 <0.01 U/U%
Storage condition below -20℃ protected from light

特性

Molecular weight ca. 90 kDa (SDS-PAGE)
Structure monomer, one mole of FAD per mole of enzyme glycoprotein
Michaelis constant 6.4×10-2M (D-glucose)
pH Optimum 7.0–7.5
pH Stability 2.5–9.5
Optimum temperature 45℃
Thermal stability (liquid form) below 60℃
Thermal stability (powder form) stable at 30℃ for at least one month
Inhibitors Mn2+, Ag+
Specificity D-glucose (100%), maltose (0.2%), 
D-xylose (0.9%), D-galactose (0.8%) 
sucrose (<0.1%),  D-mannose (0.4%)
2-deoxy-D-glucose (23.5%)

适用类型

FADGDH-AD is useful for the determination of D-glucose in clinical analysis and continuous glucose monitoring (CGM) meter for diabetes patients. The FADGDH-AD was developed as an oxygen-insensitive alternative to Glucose oxidase (GOD) with its high stability for the applications such as bioelectrodes in glucose sensing device and glucose enzymatic fuel cells.

Line-up

  • Glucose Dehydrogenase (FADGDH-AB)

参考文献

Satake R, Ichiyanagi A, Ichikawa K, Hirokawa K, Araki Y, Yoshimura T, Gomi K (2015)
Novel glucose dehydrogenase from Mucor prainii: Purification, characterization, molecular cloning and gene expression in Aspergillus sojae
Biosci Bioeng., 120, 498-503

Masakari Y, Hara C, Araki Y, Gomi K, Ito K (2020)
Improvement in the thermal stability of Mucor prainii-derived FAD-dependent glucose dehydrogenase via protein chimerization 
Enzyme Microb Technol., 132, 109387, doi: 10.1016/j.enzmictec.2019.109387.
https://doi.org/10.1016/j.enzmictec.2019.109387, (cited 2020-07-02)

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日本kikkoman龟甲万alpha-Glucosidase (αGLS-SE) α- 葡糖苷酶

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alpha-Glucosidase (αGLS-SE) α- 葡糖苷酶

  • 临床检测用酶

The enzyme is useful for the determination of α-amylase and serum chloride in clinical analysis.

由来 recombinant E. coli
系统名称

α-D-Glucoside glucohydrolase
EC编号 3.2.1.20
反应式

α-D-Glucoside + H2O →→→ α-D-Glucose + ROH

规格

Appearance white lyophilizate
Activity ≧10 U/mg
Stabilizer bovine serum albumin
Storage condition below -20℃

特性

Molecular weight ca. 61 kDa (gel filtration)
Structure monomer of 60 kDa (SDS-PAGE)
Michaelis constant 5.5×10-5M (p-nitrophenyl-α-D-glucoside)
pH Optimum 6.0–9.0
pH Stability 5.0–10.0
Optimum temperature 52–55°C
Thermal stability below 50℃
Stability (liquid form) stable at 37℃ for at least two weeks
Stability (powder form) stable at 30℃ for at least one month
Inhibitors Hg2+，Ag+
Specificity Refer to the table shown below.
Specificity
Substrate*a Relative activity (%)*b
PNPG 100.0
PNPG2 9.4
PNPG5 1.1
maltose 10.2
maltotriose 112.9
maltotetraose 13.9
maltopentaose 1.4

a：Substrate concentration, 2.2 mM

b：Glucose-forming activity, pH 7.0 at 37℃

适用类型

The enzyme is useful for the determination of α-amylase and serum chloride in clinical analysis.

参考文献

  • Halvorson, H., “Methods in Enzymology,” Vol. 8, Academic Press, New York, 1966, pp. 559–562.
  • Ono, T. et al., Clin. Chem., 34, 552–553 (1988).
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日本kikkoman龟甲万Glutaminase(GLN) 谷氨酰胺酶

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Glutaminase(GLN) 谷氨酰胺酶

  • 临床检测用酶

The enzyme is useful for the determination of L-glutamine in clinical analysis.

由来 from microorganism
系统名称

L-Glutamine amidohydrolase
反应式

L-Glutamine + H2O →→→ L-Glutamineate + NH3

规格

Appearance light gray lyophilizate
Activity ≧4 U/mg
Contaminants Catalase ≦3.0 U/U%
Stabilizer sucrose
Storage condition below – 20℃

特性

Molecular weight ca. 58 kDa (gel filtration)
Structure heterodimer (45 kDa and 22 kDa) (SDS-PAGE)
Michaelis constant  5.5×10-4 M (L-glutamine)
pH Optimum ca. 7.0
pH Stability 5.5–9.0
Optimum temperature ca. 65℃
Thermal stability below 50℃
Stability (liquid form) stable at 37℃ for at least four days
Stability (powder form) stable at 30℃ for at least two weeks
Specificity L-glutamine (100), D-glutamine (70), L-asparagine (0), D-asparagine (0)

适用类型

The enzyme is useful for the determination of L-glutamine in clinical analysis.

参考文献

Roberts, E., “The Enzymes,” Vol. 4 (2nd ed.), Academic Press, New York and London, 1960, pp. 285–300.

Hartman, S. C., “The Enzymes,” Vol. 4 (3rd ed.), Academic Press, New York and London, 1971, pp. 79–100.

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日本kikkoman龟甲万Glutamine Synthetase (GST) 谷氨酰胺合成酶

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Glutamine Synthetase (GST) 谷氨酰胺合成酶

  • 临床检测用酶

The enzyme is useful for the determination of ammonia and ATP in clinical analysis.

由来 microorganism
系统名称

L-Glutamate : ammonia ligase (ADP-forming)
EC编号 6.3.1.2
反应式

ATP + L-Glutamate + NH3→→→ ADP + Orthophosphate + L-Glutamine

规格

Appearance white to light yellow lyophilizate
Activity ≧15.0 U/mg
Contaminants Catalase ≦0.5 U/U％
Stabilizer sucrose
Storage condition below-20℃

特性

Molecular weight ca. 900 kDa (gel filtration)
Structure 57 kDa (SDS-PAGE)
Isoelectric point 6.5
Michaelis constant 1.5×10-2M (L-glutamate)
1.3×10-4M (ammonia)
8.7×10-4M (ATP)
pH Optimum ca. 7.0
pH Stability 6.5–9.5
Optimum temperature 60℃
Thermal stability below 40℃
Inhibitors methionine sulfoximine, carbamyl phosphate
Activators Mg2+，Mn2+
Specificity L-glutamate (100), D-glutamate (0.8)
NH₃(100), NH₂OH (12)
ATP (100), GTP (2.5)

适用类型

The enzyme is useful for the determination of ammonia and ATP in clinical analysis.

参考文献

Ebner, E. et al., “Methods in Enzymology,” Vol. 17A, Academic Press, New York, 1970, pp. 910–922.

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日本kikkoman龟甲万Lactate Dehydrogenase (LDH-P) 乳酸脱氢酶

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Lactate Dehydrogenase (LDH-P) 乳酸脱氢酶

  • 临床检测用酶

The enzyme is useful for the determination of numerous metabolites (ATP, ADP, glucose, creatinine, pyruvate,lactate and glycerol) and of enzyme activities (GPT, PK and CPK) when coupled with the related enzymes.

由来 porcine heart
系统名称

(S )-Lactate : NAD+ oxidoreductase
EC编号 1.1.1.27
反应式

Pyruvate + NADH + H+ L-Lactate + NAD+

规格

Appearance white lyophilizate
Activity ≧150 U/mg
Storage condition below -20℃

特性

Molecular weight ca. 115 kDa (gel filtration)
Michaelis constant 2.5×10-2M (fructosyl-glycine)
1.0×10-4M (pyruvate)
pH Optimum 7.4–8.0
pH Stability 7.0–7.5
Optimum temperature 50–55℃
Thermal stability below 45℃

适用类型

The enzyme is useful for the determination of numerous metabolites (ATP, ADP, glucose, creatinine, pyruvate, lactate and glycerol) and of enzyme activities (GPT, PK and CPK) when coupled with the related enzymes.

参考文献

  • Jaenicke, R. and Pfleiderer, G., Biochim. Biophys. Acta, 60, 615 (1962).
  • Everse, J. and Kaplan, N. O., Adv. in Enzymol., 37, 61 (1973).
  • Holbrook, J. J. et al., “The Enzyme,” Vol. 11 (3rd ed.), Academic Press, New York and London, 1975, pp. 191–292.
  • Loshon, C. A. et al., Clin.Chem., 23, 1579 (1977).
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日本kikkoman龟甲万Maltose Phosphorylase (MPL-EP) 麦芽糖磷酸化酶

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Maltose Phosphorylase (MPL-EP) 麦芽糖磷酸化酶

  • 临床检测用酶

The enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.

由来 recombinant E. coli
系统名称

Maltose : orthophosphate 1-β-D-glucosyltransferase
EC编号 2.4.1.8
反应式

Maltose + Orthophosphate →→→ D-Glucose + β-D-Glucose 1-phosphate

规格

Appearance white lyophilizate
Activity ≧10 U/mg
Stabilizer lactose, ethylenediaminetetraacetic acid (EDTA)
Storage condition below -20℃

特性

Molecular weight

ca. 220 kDa (gel filtration)
Structure 2 subunits of 90 kDa (SDS-PAGE)
Michaelis constant

1.9×10-3M (maltose)

3.4×10-3 M (phosphate)

8.3×10-3M (arsenate)
pH Optimum 6.5–7.5
pH Stability 5.5–8.0
Optimum temperature 45–50°C
Thermal stability below 55℃
Stability (liquid form) stable at 37℃ for at least one week
Stability (powder form) stable at 30℃ for at least four weeks
Inhibitors

Hg2+，Ag+，Zn2+，Cu2+

适用类型

The enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.

参考文献

  • Hiruma, M. et al., Nippon Nogeikagaku Kaishi, 70, 773–780 (1996).
  • Shirokane, Y. et al., Carbohydr. Res., 329, 699–702 (2000).
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日本kikkoman龟甲万beta-Phosphoglucomutase (βPGM-EP) β- 磷酸葡糖变位酶

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beta-Phosphoglucomutase (βPGM-EP) β- 磷酸葡糖变位酶

  • 临床检测用酶

The enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.

由来 recombinant E. coli
系统名称

β-D-Glucose 1,6-phosphomutase
EC编号 5.4.2.6
反应式

β-D-Glucose 1-phosphate →→→ β-D-Glucose 6-phosphate

规格

Appearance white lyophilizate
Activity ≧30 U/mg
Stabilizer lactose,  ethylenediaminetetraacetic acid (EDTA)
Storage condition below -20℃

特性

Molecular weight ca. 34 kDa (gel filtration)
Structure monomer of ca. 25 kDa (SDS-PAGE)
Michaelis constant 2.3×10-4M (β-D-glucose-1-phosphate)
pH Optimum ca. 7.0
pH Stability 5.0–9.5
Optimum temperature 40℃
Thermal stability below 45℃
Stability (liquid form) stable at 37℃ for at least one week
Stability (powder form) stable at 30℃ for at lest one month
Activators Mg2+，Mn2+，Co2+，Ni2+
Inhibitors

Hg2+，Zn2+，Cu2+，Cd2+

适用类型

The enzyme is useful for the determination of α-amylase and inorganic phosphate in clinical analysis.

参考文献

  • Nakamura, K. et al., J. Ferment. Bioeng., 85, 350–353 (1998).
  • Shirokane, Y. et al., Carbohydr. Res., 329, 699–702 (2000).
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日本kikkoman龟甲万Sarcosine Oxidase (SOD-TE) 肌氨酸氧化酶

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Sarcosine Oxidase (SOD-TE) 肌氨酸氧化酶

  • 临床检测用酶

The enzyme is useful for the determination of creatinine and creatine in clinical analysis.

由来 recombinant E. coli
系统名称

Sarcosine : oxygen oxidoreductase (demethylating)
EC编号 1.5.3.1
反应式

Sarcosine + H2O + O2 →→→ Glycine + Formaldehyde + H2O2

规格

Appearance yellow lyophilizate
Activity ≧20 U/mg
Contaminants Creatininase　<1.0×10-2 U/U%
Stabilizer sucrose 
Storage condition below -20℃ protected from light

特性

Molecular weight ca. 49 kDa (gel filtration)
Structure monomer of 43 kDa (SDS-PAGE)
one mole of FAD per mole of enzyme
Isoelectric point 5.3
Michaelis constant 4.7×10-3M (sarcosine)
pH Optimum 6.7–9.5
pH Stability 6.5–10.5
Optimum temperature 50℃
Thermal stability below 55℃
Stability (liquid form) stable at 37℃ for at least two weeks
Stability (powder form) stable at 30℃ for at least one month
Inhibitors Zn2+，Cu2+，Hg2+，Ag+

适用类型

The enzyme is useful for the determination of creatinine and creatine in clinical analysis.

参考文献

Suzuki, M. and Yoshida, M. (1984)
A new enzymatic determination of serum creatine
Clinica Chimica Acta, 140, 289–294.

Suzuki, M. and Yoshida, M. (1984)
A new enzymatic serum creatinine measurement based on an endogenous creatine-eliminating system
Clinica Chimica Acta, 143, 147–155.

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日本kikkoman龟甲万Sucrose Phosphorylase (SPL-E) 蔗糖磷酸化酶

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Sucrose Phosphorylase (SPL-E) 蔗糖磷酸化酶

  • 临床检测用酶

The enzyme is useful for the determination of inorganic phosphate in clinical analysis.

由来 recombinant E. coli
系统名称

Sucrose : orthophosphate α-D-glucosyltransferase
EC编号 2.4.1.7
反应式

Sucrose + Orthophosphate →→→ D-Fructose + α-D-Glucose 1-phosphate

规格

Appearance white lyophilizate
Activity ≧50 U/mg
Stabilizer sucrose
Storage condition below -20℃

特性

Molecular weight ca. 56 kDa (gel filtration)
Structure monomer of 56 kDa (SDS-PAGE)
Isoelectric point 4.6
Michaelis constant 3.9×10-2M (sucrose)
6.2×10-3M (phosphate)
pH Optimum 7.5
pH Stability 5.0–8.0
Optimum temperature 40℃
Thermal stability below 45℃
Stability (liquid form) stable at 37℃ for at least two weeks
Stability (powder form) stable at 30℃ for at least two weeks
Inhibitors glucose, glucono-1,5-lactone
Specificity sucrose (100), maltose (0), starch (0)

适用类型

The enzyme is useful for the determination of inorganic phosphate in clinical analysis.

参考文献

  • Koga, T. et al., Agric. Biol. Chem., 55, 1805–1810 (1991).
  • Kitao, S. and Nakano, E., J. Ferment. Bioeng., 73, 179–184 (1992).
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  • SDS

日本kikkoman龟甲万Urease (URE) 尿素酶

发表于由

上海金畔生物科技有限公司代理龟甲万酶制剂全线产品，欢迎访问官网了解更多信息。

Urease (URE) 尿素酶

  • 临床检测用酶

The enzyme is useful for the determination of urea in clinical analysis.

由来 jack bean
系统名称

Urea amidohydrolase
EC编号 3.5.1.5
反应式

Urea +H2O →→→ CO2 +2NH3

规格

Appearance yellow lyophilizate
Activity ≧100 U/mg
Stabilizer lactose, ethylenediaminetetraacetic acid (EDTA), DTE
Storage condition below-20℃

特性

Molecular weight ca. 480 kDa (gel filtration)
Structure 8 subunits (containing nickel)
Isoelectric point 5.0–5.1
Michaelis constant 1.05×10-2M (urea)
pH Optimum ca. 8.0
pH Stability 5.0–10.0
Optimum temperature 60℃
Thermal stability below 50℃
Inhibitors heavy metal ions，Na+，K+，NH₄+，suramin, thiourea
Specificity specific for urea

适用类型

The enzyme is useful for the determination of urea in clinical analysis.

参考文献

  • Sumner, J. B. and Hand, D. B., J. Am. Chem. Soc., 51, 1255–1260 (1929).
  • Gorin, G. and Chin, C., Biochim. Biophys. Acta, 99, 418–426 (1965).
  • Fishbein, W. N. et al., J. Biol. Chem., 245, 5985–5992 (1970).
  • Fishbein, W. N. and Nagarajan, K., Arch. Biochem. Biophys., 144, 700–714 (1971).
  • Contaxis, C. and Reithel, F. J., Canadian J. Biochem., 50, 461–473 (1972).
  • Schlegel, H. and Kaltwasser, H., “Methods of Enzymatic Analysis,” Vol. 2 (2nd ed.), Verlag Chemie, Weinheim,Germany, 1974, pp. 1081–1085.
  • Bergmeyer, H. U., “Methods of Enzymatic Analysis,” Vol. 2 (3rd ed.), Verlag Chemie, Weinheim, Germany, 1983,pp. 320–321.
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  • SDS

日本kikkoman龟甲万Uricase (U-TE) 尿酸酶

发表于由

上海金畔生物科技有限公司代理龟甲万酶制剂全线产品，欢迎访问官网了解更多信息。

Uricase (U-TE) 尿酸酶

  • 临床检测用酶

The enzyme is useful for the determination of uric acid in clinical analysis.

由来 recombinant E. coli
系统名称

Urate : oxygen oxidoreductase
EC编号 1.7.3.3
反应式

Urate + H2O + O2 →→→ Unidentified products + H2O2

　　　　　　　　　　　　　↓

　　　　　　　　　　 　　CO2 + Allantoin (racemic mixture)

规格

Appearance light brownish lyophilizate
Activity ≧4.0 U/mg
Contaminants Catalase　≦1.0 U/U%
Stabilizer sucrose, citrate, ethylenediaminetetraacetic acid (EDTA)
Storage condition below -20℃

特性

Molecular weight ca. 90 kDa (gel filtration)
Structure 2 subunits of 35 kDa (SDS-PAGE)
Michaelis constant 1.1×10-5M (uric acid)
pH Optimum 8.5
pH Stability 7.0–11.0
Optimum temperature 45℃
Thermal stability below 55℃
Stability (liquid form) stable at 37℃ for at least ten days
Stability (powder form) stable at 30℃ at least three weeks
Inhibitors Hg2+，Ag+

适用类型

The enzyme is useful for the determination of uric acid in clinical analysis.

参考文献

Koyama, Y. et al., J. Biochem., 120, 969–973 (1996).

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  • SDS

日本kikkoman龟甲万LuciPac A3 Surface Pre-moistened（湿润棉棒） 60367

发表于由

上海金畔生物科技有限公司代理龟甲万酶制剂全线产品，欢迎访问官网了解更多信息。

LuciPac A3 Surface Pre-moistened（湿润棉棒） 60367

  • ATP荧光检测

LuciPac A3 Surface Pre-moistened（湿润棉棒） 60367

LuciPac A3 Surface Pre-moistened（湿润棉棒）不仅能检测 ATP，连同 ADP+AMP 也能检测出来，是一款预先湿润的涂抹棒和试剂一体化的高灵敏度检测试剂。

包装形态 100 支/包 (20支/铝箔袋 x 5)
保存条件 2-8 ℃ (切勿冷冻)
有效期限

生产日期起8个月

注意事项

  • 本款试剂是Lumitester Smart/PD-30/PD-20的专用试剂 ，其他品牌的机器不能使用。
  • 请勿在检查清洁度以外的目的使用本产品。
  • 本产品不可用于活菌、特定病原菌等检测。
  • 产品单页
  • 使用说明书
  • SDS

日本龟甲万酶试剂 Enzymes for Clinical Chemistry

发表于由

日本龟甲万酶试剂 Enzymes for Clinical Chemistry
kikkoman キッコーマンバイオケミファ株式会社

闻名全球的日本佐料制造商及供应商龟甲万（Kikkoman）公司率先推出的ATP荧光检测仪，直接采用ATP荧光度来衡量细菌多少，机身轻巧，价格实惠，操作简单、快速，只要简单说明，员工即可在10秒内完成对产品细菌量的检测！
日本龟甲万酶试剂 Enzymes for Clinical Chemistry
Product Code Origin Activity (more than)
A Alkaline Phosphatase (ALP)PDF – calf intestinal mucosa 6000 U/mg protein
C Catalase (CAT)PDF 61152 bovine liver 12,000 U/mg lyophilizate
Cholesterol Esterase (CHE-XE)*PDF 60468 recombinant E. coli 5 U/mg lyophilizate
Cholesterol Oxidase (CHO-CE)*PDF 60266 recombinant E. coli 5 U/mg lyophilizate
Cholesterol Oxidase (CHO-PEWL)PDF 60271 recombinant E. coli 200 U/ml
Creatinase (C2-AE)PDF 60108 recombinant E. coli 9 U/mg lyophilizate
Creatinase (C2-AT)PDF 60118 recombinant E. coli 9 U/mg lyophilizate
Creatininase (C1- E)PDF 60111 recombinant E. coli 600 U/mg lyophilizate
F Fructosyl-amino Acid Oxidase (FAOX-TE)*PDF 60242 recombinant E. coli 1.0 U/mg lyophilizate
Fructosyl-amino Acid Oxidase (FAOD-E)*PDF 60273 recombinant E. coli 4 U/mg lyophilizate
Fructosyl-peptide Oxidase (FPOX-CE)PDF 60123 recombinant E. coli 6 U/mg yophilizate
Fructosyl-peptide Oxidase (FPOX-CET)*PDF 60131 recombinant E. coli 5.0 U/mg lyophilizate
G Glucose Dehydrogenase (FADGDH-AA)PDF 60100 recombinant A. sojae 500 U/mg lyophilizate
alpha-Glucosidase (aGLS-SE)PDF 60241 recombinant E. coli 10 U/mg lyophilizate
Glutamine Synthetase (GST)PDF 61222 microorganism 7 U/mg lyophilizate
H 3alpha-Hydroxysteroid Dehydrogenase (3aHSD-EH)*PDF 61224 recombinant B.choshinensis 30 U/mg lyophilizate
L Lactate Dehydrogenase (LDH-P)PDF 61170 porcine heart 150 U/mg lyophilizate
Maltose Phosphorylase (MPL-EP)PDF 60233 recombinant E. coli 10 U/mg lyophilizate
P beta-Phosphoglucomutase (bPGM-EP)PDF 60189 recombinant E. coli 30 U/mg lyophilizate
S Sarcosine Oxidase (SOD-TE)PDF 60105 recombinant E. coli 15 U/mg lyophilizate
Sucrose Phosphorylase (SPL-E)PDF 60122 recombinant E. coli 20 U/mg lyophilizate
U Urease (URE)PDF 61156 jack bean 100 U/mg lyophilizate
Uricase (U-TE)PDF