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Isolation and partial characterization of molecular forms of ceruloplasmin from human bile
Author(s) -
Verbina Irene A.,
Puchkova Ludmila V.,
Gaitskhoki Vladimir S.,
Neifakh Solomon A.
Publication year - 1992
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(92)80032-c
Subject(s) - ceruloplasmin , molecular mass , biochemistry , chemistry , oxidase test , proteolysis , affinity chromatography , isolation (microbiology) , microbiology and biotechnology , enzyme , biology
Highly purified ceruloplasmin (CP) was isolated from human bile using affinity chromatography. Billiary CP is represented by two molecular species. One of those is identical to oxidase CP from normal human serum while the other is analogous to oxidase‐lacking CP specific for the serum of the carriers of Wilson's mutation with respect to immunological specificity, electrophoretical mobility and molecular mass of the large fragments from spontaneous proteolysis.