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Citrate in urine determined with a new citrate lyase method
M Petrarulo1, P Facchini, E Cerelli
1Renal Stone Laboratory, Mauriziano Umberto I Hospital, Turin, Italy.
Clinical Chemistry
|October 1, 1995
Summary
A new spectrophotometric method accurately measures citrate in biological fluids using citrate lyase and phenylhydrazine. This simpler, cheaper assay is more sensitive and precise than traditional methods for citrate determination.
Area of Science:
- Biochemistry
- Analytical Chemistry
- Clinical Diagnostics
Background:
- Citrate determination is crucial for diagnosing various metabolic disorders.
- Existing methods for citrate quantification can be complex, costly, or lack sensitivity.
Purpose of the Study:
- To develop a novel, efficient, and cost-effective enzyme-spectrophotometric method for quantifying citrate in biological samples.
- To enhance sensitivity and precision compared to established citrate assays.
Main Methods:
- Utilized citrate lyase to convert citrate to oxaloacetate.
- Employed phenylhydrazine to form a phenylhydrazone derivative of oxaloacetate.
- Measured the ultraviolet absorbance of the product at 330 nm for quantification.
Main Results:
- The proposed method demonstrated higher precision and twice the sensitivity of the traditional citrate lyase method.
- Analytical recovery of citrate averaged 100.7% ± 2.2%.
- The assay exhibited low imprecision (CV 2.0% at 0.96 mmol/L) and a lower limit of quantification of 0.08 mmol/L.
- Results showed good correlation with ion-chromatographic and traditional citrate lyase methods.
Conclusions:
- The developed enzyme-spectrophotometric method offers a simpler, cheaper, and more sensitive alternative for biological citrate determination.
- This assay is suitable for routine clinical and research applications requiring accurate citrate quantification.