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Electrophoretic properties of radioiodine‐labelled human serumalbumin at different iodination degrees
Author(s) -
Ambrosino C.,
Scassellati G. A.,
Papa G.,
Rosa U.
Publication year - 1967
Publication title -
journal of labelled compounds
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.432
H-Index - 47
eISSN - 1099-1344
pISSN - 0022-2135
DOI - 10.1002/jlcr.2590030503
Subject(s) - electrophoresis , chemistry , iodine , human serum albumin , homogeneous , halogenation , chromatography , albumin , biochemistry , organic chemistry , thermodynamics , physics
Progressive iodination of HSA affects its electrophoretic behaviour : however, no apparent formation of degradation products has been detected up to a substitution degree of about 24 iodine atoms per molecule of HSA. The HSA, progressively iodinated, shows an increased mobility on agar gel, and behaves as a single and homogeneous compound by moving boundary electrophoresis. No apparent correlation exists between the electrophoretic behaviour and the biological properties of the iodoalbumins which have been previously checked in humans. On this basis, the validity of electrophoresis as a control tool for the labelled albumin may be seriously questioned.