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C2409 Sigma-Aldrich

Creatinase from Actinobacillus sp.

lyophilized powder, 20-40 units/mg protein

Synonym: Creatine Amidinohydrolase

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Description

General description

Creatinase is a homodimer that catalyzes hydrolysis of creatine. It consists of two monomer subunit and two defined domains; N and C terminal domains. C terminal fold have both the α helices and anti-parallel β sheet within two structurally similar domains. In between these two domains, there is a sulfhydryl group that acts as active site and the activity is metal independent.

Application

Creatinase mixed with sarcosine oxidase may be used to determine the level of creatine in different pH, temperature, enzyme ratio, and buffer concentration. It may also be used to determine the plasma creatinine level by using a centrifugal analyser.

Packaging

1000 units in poly bottle

Biochem/physiol Actions

Creatinase accelerates the conversion reaction of creatine and water molecule to sarcosine and urea. It always acts in homodimer state and is induced by choline chloride.

Physical properties

Isoelectric point: 4.6 ± 0.1
Michaelis constant: 1.9 x 10‾2M (Creatine)
Structure: 2 subunits per mole of enzyme
Inhibitors: Cu++, Hg++, Ag+
Optimum pH: 8.0
Optimum temp: 40°C
pH Stability: pH 5.5 − 9.0 (25°C, 16hr)
Thermal stability: Below 50°C (pH 7.5, 30 min)

Unit Definition

One unit will hydrolyze 1.0 μmole of creatine to urea and sarcosine per min at pH 7.5 at 37 °C.

Physical form

Lyophilized powder containing sugars and EDTA as stabilizers

Safety & Documentation

Safety Information

Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis (COA)

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Certificate of Origin (COO)

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Protocols & Articles

Protocols

Assay Procedure for Creatinase

The appearance of yellow dye formed by condensation of urea and p-dimethylaminobenzaldehyde (DAB) (Ehrlich reaction) is measured at 435nm by spectrophotometry.
Keywords: Condensations, Extinction coefficient

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Peer-Reviewed Papers
15

References

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