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Differences in the isoelectric focusing patterns of serum and cerebrospinal fluid transthyretin
Author(s) -
Szilágyi A. Katalin,
Ha Nguyen Thu,
Szetényi Judit,
Puskás Éva
Publication year - 1993
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.11501401172
Subject(s) - transthyretin , isoelectric focusing , cerebrospinal fluid , isoelectric point , chemistry , polyacrylamide gel electrophoresis , two dimensional gel electrophoresis , electrophoresis , biochemistry , chromatography , biology , endocrinology , gene , enzyme , proteomics , neuroscience
Transthyretin isolated by polyacrylamide gel electrophoresis from human serum and cerebrospinal fluid, dissociated into its subunits, was subjected to isoelectric focusing in polyacrylamide gels containing 8 mole/L urea. The isoelectric focusing multi‐component patterns of serum and cerebrospinal fluid transthyretin differ in a characteristic way, having only one main protein zone in common. Double diffusion immunotest and immunoblotting revealed the immunological identity of serum and cerebrospinal fluid transthyretin and of the main components separated by isoelectric focusing. The different isoelectric focusing zones can be consistently explained when they are ascribed to structurally identical transthyretin subunits associated with different ligands specifically occurring in either serum or cerebrospinal fluid. Only the protein zone located at the same p I , in serum and cerebrospinal fluid transthyretin patterns may be assigned to ligand‐free subunits. Thus, the typical differences in isoelectric focusing patterns may point to different carrier functions of transthyretin in serum and cerebrospinal fluid.