Evaluation of albumin structural modifications through cobalt-albumin binding (CAB) assay

Eunyoung Lee, Ji Eun Eom, Kyung Hwa Jeon, Tae Hee Kim, Eunnam Kim, Gil Ja Jhon, Youngjoo Kwon

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

Human serum albumin (HSA) is the most abundant protein in the human body. HSA injections prepared by fractionating human blood have mainly covered the demand for albumin to treat hypoalbuminemia, the state of low concentration of albumin in blood. HSA in solution may exist in various forms such as monomers, oligomers, polymers, or as mixtures, and its conformational change and/or aggregation may occur easily. Considering these characteristics, there is a great chance of modification and polymer formation during the preparation processes of albumin products, especially injections. The albumin cobalt binding (ACB) test reported by Bar-Or et al. was originally designed to detect ischemia modified albumin (IMA), which contains the modified HSA N-terminal sequence by cleavage of the last two amino acids. In this study, we developed a cobalt albumin binding (CAB) assay to correct the flaws of the ACB test with improving the sensitivity and precision. The newly developed CAB assay easily detects albumin configuration alterations and may be able to be used in developing a quality control method for albumin and its pharmaceutical formulations including albumin injections.

Original languageEnglish
Pages (from-to)17-23
Number of pages7
JournalJournal of Pharmaceutical and Biomedical Analysis
Volume91
DOIs
StatePublished - 25 Mar 2014

Keywords

  • 96-Well volume reaction
  • Albumin conformational change
  • Cobalt albumin binding (CAB) assay
  • Nitrogen monoxide

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