HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Submit an electronic Letter to the Editor about this paper Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in ISI Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (7) Citing Articles via Google Scholar Google Scholar Articles by Balion, C. M. Articles by Ali, A. C. Y. Search for Related Content PubMed PubMed Citation Articles by Balion, C. M. Articles by Ali, A. C. Y. Related Collections General Clinical Chemistry Oak Ridge Conference Drug Monitoring and Toxicology

Evaluation of HemogloBind^TM for Removal of o-Raffinose Cross-Linked Hemoglobin (Hemolink^TM) from Serum

^a author for correspondence: fax 416-798-0152

Hemoglobin-based oxygen carriers (HBOCs) are now undergoing extensive clinical trials to determine their therapeutic potential (1). HBOCs in plasma resemble massive hemoglobinemia and create a challenge for the chemistry laboratory to accurately measure analytes in their presence. Hemolink^TM, like hemoglobin and other HBOCs, has been found to interfere with common laboratory test methodologies (2). Interference from HBOCs is caused by an increase in absorbance or by interference in certain chemical reactions (e.g., peroxidase-like activity) (3)(4). It is therefore necessary to measure affected serum analytes by alternative methods, utilize correction factors, or remove the interfering HBOC to obtain accurate results (5)(6)(7). Hemolink comprises a mixture of stabilized human hemoglobin molecules (64–600 kDa). Periodate-oxidized raffinose (o-raffinose) cross-links the ß-subunits at Lys-82 to form stabilized hemoglobin tetramers, and in addition intermolecularly cross-links tetramers through surface amino groups to form hemoglobin polymers.

Recently, a new product that has been reported to selectively bind and remove free hemoglobin from clinical samples has come onto the market. HemogloBind^TM is an insoluble anionic polyelectrolyte manufactured by LigoChem (Fairfield, NJ). The application of HemogloBind for the removal of Hemolink and other HBOCs would reduce the potential for interference in laboratory methods. The objective of this study was to evaluate the efficiency of HemogloBind in removing Hemolink from serum. Parallel experiments were also done with highly purified human hemoglobin (HemAzero^TM).

To pooled human serum . . . [Full Text of this Article]

Footnotes

References

The following articles in journals at HighWire Press have cited this article:

				A. A. Ali, G. S. Ali, J. M. Steinke, and A. P. Shepherd Co-Oximetry Interference by Hemoglobin-Based Blood Substitutes Anesth. Analg., April 1, 2001; 92(4): 863 - 869. [Abstract] [Full Text] [PDF]

				Z. Ma, T. G. Monk, L. T. Goodnough, A. McClellan, M. Gawryl, T. Clark, P. Moreira, P. E. Keipert, and M. G. Scott Effect of hemoglobin- and Perflubron-based oxygen carriers on common clinical laboratory tests Clin. Chem., September 1, 1997; 43(9): 1732 - 1737. [Abstract] [Full Text] [PDF]