TY - JOUR
T1 - Evaluation of albumin structural modifications through cobalt-albumin binding (CAB) assay
AU - Lee, Eunyoung
AU - Eom, Ji Eun
AU - Jeon, Kyung Hwa
AU - Kim, Tae Hee
AU - Kim, Eunnam
AU - Jhon, Gil Ja
AU - Kwon, Youngjoo
N1 - Funding Information:
This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology ( 2011K000813 ).
PY - 2014/3/25
Y1 - 2014/3/25
N2 - 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.
AB - 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.
KW - 96-Well volume reaction
KW - Albumin conformational change
KW - Cobalt albumin binding (CAB) assay
KW - Nitrogen monoxide
UR - http://www.scopus.com/inward/record.url?scp=84892473600&partnerID=8YFLogxK
U2 - 10.1016/j.jpba.2013.12.003
DO - 10.1016/j.jpba.2013.12.003
M3 - Article
C2 - 24434278
AN - SCOPUS:84892473600
SN - 0731-7085
VL - 91
SP - 17
EP - 23
JO - Journal of Pharmaceutical and Biomedical Analysis
JF - Journal of Pharmaceutical and Biomedical Analysis
ER -