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The behavior of serum albumin upon isoelectric focusing on immobilized pH gradients
Author(s) -
Gianazza Elisabetta,
Frigerio Adele,
AstruaTestori Silvia,
Righetti Pier Giorgio
Publication year - 1984
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.1150050512
Subject(s) - isoelectric focusing , albumin , chromatography , chemistry , isoelectric point , saturation (graph theory) , serum albumin , biochemistry , enzyme , mathematics , combinatorics
Isoelectric focusing on immobilized pH gradients dissociates most complexes between fatty acids and serum albumin from whole plasma. Most albumin thus migrates to a pI of 5.8, very close to the theoretical value of 6.0 as calculated with the Linderstrøm‐Lang equation. The phenomenon was elucidated through saturation experiments and time‐course monitoring of the protein pattern upon focusing.