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Change of human hemopexin isoelectric point upon heme binding
Author(s) -
Plancke Y.,
Dautrevaux M.,
Biserte G.
Publication year - 1977
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(77)80326-8
Subject(s) - hemopexin , physics , humanities , chemistry , philosophy , heme , biochemistry , enzyme
Hemopexin is the serum /.I-glycoprotein with a high affinity for heme [ 1 ] and its biological and physicochemical properties have been reviewed by MullerEberhard and Liem [2]. The detailed characterization of the protein is hampered by the complexity and low yields of the isolation procedures, specially for human hemopexin [3-51. In an attempt to explain differences in purification procedures of human hemopexin, we present here experimental evidence for a change in its isoelectric point upon heme-binding. It provides information on the change in the conformation of hemopexin induced by its interaction with heme and thus may contribute for understanding the means by which hemopexin fulfills its physiological function in heme transport.