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Transient bisalbuminemia: Separation by isoelectric focusing of human albumin fractions linked to different numbers of benzylpenicilloyl groups
Author(s) -
Rocha Jorge,
Bohner Jürgen,
Kömpf Jost
Publication year - 1995
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.11501601174
Subject(s) - isoelectric focusing , human serum albumin , urea , chemistry , chromatography , covalent bond , residue (chemistry) , isoelectric point , albumin , conjugated system , lysine , biochemistry , organic chemistry , amino acid , polymer , enzyme
Abstract The behavior of modified human serum albumin (HSA) from penicillin‐treated patients and in vitro conjugated samples was studied by isoelectric focusing in the absence and presence of 8 M urea. It is shown that samples classified as bisalbuminemic after separation under native conditions display a spectrum of several major bands with decreasing p I s when focusing is done in the presence of 8 M urea. In this spectrum, the distances between two consecutive major bands are as expected from a 2‐unit charge difference. Since this result is compatible with the blockage of a lysine residue with a benzylpenicilloyl (BPO) group, each major band can be interpreted as representing an HSA fraction covalently linked to different numbers of benzylpenicilloyl groups. The separation methods presented therefore seem to constitute simple and reliable tools for a detailed assessment of the extent of BPO covalent binding to HSA both in vivo and in vitro .