C9409
Creatinine Deiminase microbial
lyophilized powder, ≥25 units/mg protein
Sinónimos:
Creatinine Deaminase
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250 UNITS
US$ 1.290,00
US$ 1.290,00
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Disponible para envío el07 de abril de 2025Detalles
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250 UNITS
US$ 1.290,00
About This Item
Número de CAS:
Número CE:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54
US$ 1.290,00
PRECIOS SIN IMPUESTOS NACIONALES
Disponible para envío el07 de abril de 2025Detalles
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Formulario
lyophilized powder
actividad específica
≥25 units/mg protein
mol peso
~260 kDa
composición
Protein, ≥15% biuret
temp. de almacenamiento
−20°C
Aplicación
Creatinine Deiminase microbial has been used:
- to immobilize aminosilylated glass beads based biosensor for ammonia/ammonium and creatinine detection in urine[1]
- in creating creatinine-sensing membrane for biophysical studies[2]
- to investigate the bioelectronic tongue for the simultaneous determination of urea, creatinine and alkaline ions in clinical samples[3]
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.
Acciones bioquímicas o fisiológicas
Creatinine deiminase catalyzes the hydrolysis of creatinine to methylhydantoine and ammonia.[1]
Propiedades físicas
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)
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)
Definición de unidad
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.
Forma física
Lyophilized powder containing mannitol as stabilizer
Código de clase de almacenamiento
11 - Combustible Solids
Clase de riesgo para el agua (WGK)
WGK 3
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Equipo de protección personal
Eyeshields, Gloves, type N95 (US)
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Anjal C Sharma et al.
Journal of the American Chemical Society, 126(9), 2971-2977 (2004-03-05)
We developed a new sensing motif for the detection and quantification of creatinine, which is an important small molecule marker of renal dysfunction. This novel sensor motif is based on our intelligent polymerized crystalline colloidal array (IPCCA) materials, in which
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
O A Zinchenko et al.
Biosensors & bioelectronics, 35(1), 466-469 (2012-03-31)
The highly sensitive and selective potentiometric biosensor for creatinine determination has been developed by us earlier. In it, pH-sensitive field effect transistors were used as transducer and immobilized creatinine deiminase (EC 3.5.4.21)--as a biosensitive element. In the work presented, we
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
W F Stöcklein et al.
Biosensors & bioelectronics, 15(7-8), 377-382 (2001-02-24)
A procedure is described which allows the characterization of enzyme by a hybrid approach using an enzyme and an antibody. The presented method is related to the affinity determination of antibodies by the 'affinity in solution' procedure for BlAcore. The
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