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Hyaluronan‐binding properties of human serum hemopexin
Author(s) -
Hrkal Z.,
Kuzelová K.,
Muller-Eberhard U.,
Stern R.
Publication year - 1996
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(96)00225-6
Subject(s) - hemopexin , hyaluronic acid , chemistry , hyaluronidase , glycoprotein , agarose , biochemistry , electrophoresis , heme , enzyme , biology , genetics
Hemopexin, the heme‐binding serum glycoprotein, exhibits a complex electrophoretic pattern on two‐dimensional immunoelectrophoresis on agarose gels into which hyaluronic acid is incorporated in the first and monospecific anti‐hemopexin in the second dimension. This heterogeneity reflects a range of interactions of hemopexin isoforms with hyaluronic acid. Electrophoretic patterns of individual human sera greatly differ in their contents of hyaluronan‐interacting hemopexin species. Hemopexin itself has no hyaluronidase activity.