MONMOUTH JUNCTION, N.J. — Measurement of analytes in serum for the chemistry laboratory is hampered by the presence of increased hemoglobinemia caused by hemoglobin-based oxygen carriers (HBOCs) because of increased absorbance or interference in chemical reactions such as peroxidase-like activity. Researchers are conscious of the potential for assay interferences caused by hemoglobin. Many spectrophotometric methods are affected by the intense red color of serum from patients receiving doses of HBOC. Hemolysis causes strong optical absorbances of Hb species interfering the results of colorimetric and spectrophotometric methods used in clinical laboratories. Hemoglobin interference serves as a recognized source of error in laboratory medicine. Biotech Support Group’s research and development team has developed a polyelectrolyte HemogloBind™ for removing hemoglobin. Hemoglobind is suitable for use with surfactants, chaotropes, water-soluble analytes. It distinquishes between hemoglobin variants and has applications in blood substitutes, enzyme recovery, serum clarification, hemoglobin isolation, analytical protocols, thalassemia variants, red cell lysates and analytical interferences.

Similar to HBOCs, Hemolink™ interferes with lab testing of serum because it comprises of stabilized human hemoglobin molecules consisting of hemoglobin tetramers intermolecularly cross-linked by amino groups to form hemoglobin polymers. Authors Baion et al evaluated the efficiency of HemogloBind™ in removing Hemolink from serum by following the HemogloBind™ protocol.

Interesting results include:

• Hemoglobin and Hemolink(synthetic hemoglobin) can be successfully removed using HemogloBind™
• Total protein content and serum analytes such as amylase, alanine aminotransferase, alkaline phosphatase, aspartate aminotransferase, bilirubin, creatine kinase, creatinine, glucose, lactate dehydrogenase, lipase, and urea are subsequently measured.
• Increasing volumes of Hemoglobind™ decreases total protein recovery.
• When the optimal HemogloBind:serum volume ratio is alterated changes in the binding characteristics of HemogloBind are also observed.
• Lipase activity decreases after using Hemoglobind™

HemogloBind™ is engineered for a high degree of selectivity and does not cross react with most common serum components, making it an excellent tool in numerous applications for the analysis of human cytosolic and membrane sub-proteomes, removal of hemoglobin from red blood cell lysates, biomarker analysis of blood products and extraction of hemoglobin after hemolysis.

About Biotech Support Group LLC

Biotech Support Group LLC is a leading developer of proteomic and genomic sample preparation and enrichment products. Its principal products include: AlbuVoid™ for albumin depletion, Cleanascite™ for lipid adsorption and clarification, HemogloBind™ & HemoVoid™ for hemoglobin removal, NuGel™ for functional & chemical proteomics, and ProCipitate™ & ProPrep™ for nucleic acid isolation. For more information, go to www.biotechsupportgroup.com.

CONTACTS:

Dr. Swapan Roy & Matthew Kuruc
Biotech Support Group LLC
1 Deer Park Drive, Suite M
Monmouth Junction NJ 08852
732-274-2866 Worldwide
800-935-0628 North America
sales@biotechsupportgroup.com
http://www.biotechsupportgroup.com

References

• Baion, C.M. & Ali, A.C., Evaluation Of HemogloBind™ For Removal Of O-Raffinose Crosslinked Hemoglobin (Hemolink™) Clinical Chemistry September 1997 vol. 43 no. 9 1796-1798.
• Kyoungsook Park, Christopher D. Saudek, and Gerald W. Hart (2010) Increased Expression of β-N-Acetylglucosamindase (O-GlcNAcase) in Erythrocytes from Prediabetic and Diabetic Individuals. Diabetes. 59(7):1845-50.
• Delobel J., Rubin O., Prudent M., Crettaz D., Tissot J.-D., Lion N.(2010) Biomarker Analysis of Stored Blood Products: Emphasis on Pre-Analytical Issues. International Journal of Molecular Sciences. 11(11):4601-4617
• Alvarez-Llamas, G., de la Cuesta, F., Barderas, M. G., Darde, V. M., Zubiri, I., Caramelo, C. and Vivanco, F. (2009), A novel methodology for the analysis of membrane and cytosolic sub-proteomes of erythrocytes by 2-DE. ELECTROPHORESIS, 30: 4095–4108
• Datta, Pradip (2008) Effect of Hemolysis, High Bilirubin, Lipemia, Paraproteins, and System Factors on Therapeutic Drug Monitoring. Handbook of Drug Monitoring Methods, 97-109.

Suggested References

• Glick MR, Pieper J, Ryder KW. Interferencereduced methodologies for Boehringer Mannheim/Hitachi -analyzers: validation using a recombinant hemoglobin “blood substitute” product. Clin Chem 1998;44:A140-1.
• Ali ACY, Mihas CC, Campbell JA. Interference of o-raffinose cross-linked hemoglobin with three methods for serum creatinine. Clin Chem 1997;43:1738-1743.
• Leissing N, Mattia-Goldberg C, Oskroba D. Modification of clinical chemistry methods to overcome interferences from diaspirin cross-linked hemoglobin (DCLHb) [Abstract]. Clin Chem 1993;39:1144
• Christenson RH, Gregory LC, Duh S-H, et al. Hemoglobin-based blood substitutes: interference with routine chemical tests. Clin Chem 1993;39:1129
• Moore GL, Ledford ME, Merydith A. A micromodification of the Drabkin hemoglobin assay for measuring plasma hemoglobin in the range of 5–2000 mg/dL.Biochem Med 1981;26:167-173.
• Sonntag O. Haemolysis as an interference factor in clinical chemistry. J Clin Chem Clin Biochem 1986;24:127-39.
• Guder WG. Haemolysis as an influence and interference factor in clinical chemistry. J Clin Chem Clin Biochem 1986;24:125-6.
• Glick M, Ryder KW. Interferographs. Users guide to interferences in clinical chemistry instruments. Indianapolis: Science Enterprises, 1987.