Clinical Chemistry
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Clinical Chemistry 48: 204-205, 2002;
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(Clinical Chemistry. 2002;48:204-205.)
© 2002 American Association for Clinical Chemistry, Inc.


Letters

Effect of Piperacillin-Tazobactam on Clinical Capillary Zone Electrophoresis of Serum Proteins

Xavier Bossuyt1a and Willy E. Peetermans2

1 Laboratory Medicine, Immunology and
2 Internal Medicine, University Hospitals Leuven, Katholieke Universiteit Leuven, Herestraat 49, B-3000 Leuven, Belgium

aAuthor for correspondence. E-mail xavier.bossuyt{at}uz.kuleuven.ac.be.


To the Editor:

Over the last 5 years, capillary zone electrophoresis (CZE) has emerged as an automated technique for the separation of serum proteins in clinical laboratories (1)(2)(3)(4)(5). In conventional methods, quantification of the protein fractions is based on dye binding, whereas CZE uses ultraviolet detection at 214 nm for direct protein quantification via the peptide bonds. Any substance or drug that is present in serum and that absorbs at 214 nm potentially can interfere with CZE analysis. It has been reported that radio-contrast media, which absorb at 214 nm, interfere with CZE and can simulate a monoclonal component (6)(7)(8). In the present report, we describe that the antibiotic piperacillin-tazobactam (Tazocin®; Wyeth Lederle) produces a small peak at the anodal site of the ß-globulin fraction.

In Fig. 1 , panels A and C show the ß and {gamma} fractions of CZE electropherograms (Beckman Paragon CZE 2000, software version 2.21) of two samples obtained from patients who received piperacillin-tazobactam (4 g of piperacillin/500 mg of tazobactam three times per day). In the sample shown in panel C, there was a small monoclonal protein in the {gamma} region. The antibiotic was given intravenously over a 30-min period. The samples were obtained 10 min (Fig. 1A ) and 30 min (Fig. 1C ) after administration of the antibiotic. In each case, a small but distinct peak was observed at the anodal site of the transferrin peak in the ß-globulin fraction. Such a peak is absent in a normal CZE electropherogram and was not seen in the CZE electropherogram of a specimen from the same patient as in Fig. 1A collected 2 days after piperacillin-tazobactam administration (Fig. 1B ). After this time period, the antibiotic had been cleared from the blood stream. The elimination half-life of piperacillin-tazobactam is 0.7–1.2 h in patients with normal kidney function. Protein binding for piperacillin is 16% at serum concentrations of 200–300 mg/L; for tazobactam, protein binding is 20–23%. Addition of piperacillin-tazobactam to a normal serum led to the appearance in the CZE electropherogram of an abnormal peak in the same location as the extra peak observed in the electropherogram from patients receiving the antibiotic (Fig. 1D ). Parenteral administration of vancomycin (Vancocin®, 1 g twice per day; Eli Lilly) or ceftazidim (Glazidim®, 1 g three times per day; Glaxo Wellcome) did not lead to the appearance of an abnormal peak on CZE (data not shown).



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Figure 1. Effect of piperacillin-tazobactam on serum CZE.

CZE electropherograms of the ß and {gamma} regions of two samples collected 10 min (A) and 30 min (C) after administration of intravenous piperacillin-tazobactam (4 g of piperacillin/500 mg of tazobactam three times per day). The electropherograms shown in A and C are from two different patients. (B), CZE electropherogram of a specimen collected 2 days after piperacillin-tazobactam administration in the same patient as in A. (D), CZE electropherogram of a normal serum sample supplemented with 0.8 g/L piperacillin-0.1 g/L tazobactam. The arrows in A, C, and D indicate the abnormal peak.

Collectively, intravenously administered piperacillin-tazobactam produces a small peak in the ß region in CZE. Such peaks might simulate a small monoclonal protein.


References

  1. Bienvenu J, Graziani MS, Arpin F, Bernon H, Blessum C, Marchetti C, et al. Multicenter evaluation of the Paragon CZE 2000 capillary zone electrophoresis system for serum protein electrophoresis and monoclonal component typing. Clin Chem 1998;44:599-605.[Abstract/Free Full Text]
  2. Keren DF. Capillary zone electrophoresis in the evaluation of serum protein abnormalities. Am J Clin Pathol 1998;110:248-252.[Web of Science][Medline] [Order article via Infotrieve]
  3. Katzmann JA, Clark R, Sanders E, Landers JP, Kyle RA. Prospective study of serum protein capillary zone electrophoresis and immunotyping of monoclonal proteins by immunosubtraction. Am J Clin Pathol 1998;110:503-509.[Web of Science][Medline] [Order article via Infotrieve]
  4. Jolliff CR, Blessum CR. Comparison of serum protein electrophoresis by agarose gel and capillary zone electrophoresis in a clinical setting. Electrophoresis 1997;18:1781-1784.[Web of Science][Medline] [Order article via Infotrieve]
  5. Bossuyt X, Schiettekatte G, Bogaerts A, Blanckaert N. Serum protein electrophoresis by CZE 2000 clinical capillary electrophoresis system. Clin Chem 1998;44:749-759.[Abstract/Free Full Text]
  6. Arranz-Pena M-L, Gonzalez-Sagrado M, Olmos-Linares A-M, Fernandez-Garcia N, Martin-Gil F-J. Interference of iodinated contrast media in serum capillary zone electrophoresis. Clin Chem 2000;46:736-737.[Free Full Text]
  7. Bossuyt X, Mewis A, Blanckaert N. Interference of radio-opaque agents in clinical capillary zone electrophoresis. Clin Chem 1999;45:129-131.[Free Full Text]
  8. Blessum CR, Khatter N, Alter SC. Technique to remove interference caused by radio-opaque agents in clinical capillary zone electrophoresis [Letter]. Clin Chem 1999;45:1313.[Free Full Text]



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