Skip to Content
Merck
CN

C9409

Creatinine Deiminase microbial

lyophilized powder, ≥25 units/mg protein

Synonym(s):

Creatinine Deaminase

Sign In to View Organizational & Contract Pricing.

Select a Size


About This Item

CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
253-449-1
MDL number:
EC Number:
Specific activity:
≥25 units/mg protein
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

form

lyophilized powder

specific activity

≥25 units/mg protein

mol wt

~260 kDa

composition

Protein, ≥15% biuret

storage temp.

−20°C

Quality Level

General description

Isoelectric point : 4.4
Michaelis constant : 3.5 x 10‾3M (Creatinine)
Structure : 6 subunits per mol of enzyme
Inhibitors : Ag+,Hg++, o-phenanthroline,monoiodoacetate
Optimum pH : 8.5 – 9.5
Optimum temperature : 65 – 75°C
pH Stability : pH 7.0 – 11.0 (30°C, 20hr)
Thermal stability : Below 65°C (pH 7.5, 1hr)

Application

Creatinine Deiminase microbial has been used:
  • to immobilize aminosilylated glass beads based biosensor for ammonia/ammonium and creatinine detection in urine
  • in creating creatinine-sensing membrane for biophysical studies
  • to investigate the bioelectronic tongue for the simultaneous determination of urea, creatinine and alkaline ions in clinical samples

Creatinine deiminase has been used in a study to assess the application of a creatinine-sensitive biosensor for hemodialysis control. Creatinine deiminase has also been used in a study to investigate the bioelectronic tongue for the simultaneous determination of urea, creatinine and alkaline ions in clinical samples.

Biochem/physiol Actions

Creatinine deiminase catalyzes the hydrolysis of creatinine to methylhydantoine and ammonia.

Physical form

Lyophilized powder containing mannitol as stabilizer

Other Notes

One unit will hydrolyze 1.0 μmole of creatinine to N-methylhydantoin and NH3 per min at pH 7.5 at 37 °C in a coupled system with L-glutamic dehydrogenase.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

新产品
This item has

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Anne K Bendt et al.
Archives of microbiology, 181(6), 443-450 (2004-05-19)
In order to utilize different nitrogen sources and to survive situations of nitrogen limitation, microorganisms have developed several mechanisms to adapt their metabolism to changes in the nitrogen supply. In this communication, the use of creatinine as an alternative nitrogen
C M Huang et al.
Clinical chemistry, 34(1), 59-62 (1988-01-01)
We developed an enzymatic method for determination of 5-fluorocytosine in serum, using creatine iminohydrolase (EC 3.5.4.21), the Cobas-Bio analyzer, and an extant ammonia method. Analytical recovery (y) of drug added to serum (x) was good, with y = 0.97x-0.7, Sy.x
A J Killard et al.
Trends in biotechnology, 18(10), 433-437 (2000-09-22)
Creatinine biosensors, based on both potentiometric and amperometric devices, have been created. However, there are significant problems still to be addressed, including the balance between sensitivity and selectivity, interference rejection and sensor stability. In addition, many devices still rely on
L Campanella et al.
The Analyst, 115(6), 827-830 (1990-06-01)
Enzyme sensors for urea and creatinine were developed by coupling an ammonia gas-diffusion electrode with triacetate cellulose membranes entrapping urease or creatinine deiminase enzymes. Satisfactory results were obtained by using these sensors both in standard solutions and in authentic biological
[Immobilized enzyme reactors--their use in chemiluminescence detection].
M Tabata et al.
Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme, 31(3), 220-229 (1986-03-01)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service