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Expression of human recombinant β 2 ‐glycoprotein I with anticardiolipin antibody cofactor activity
Author(s) -
Kouts S.,
Bunn C.L.,
Steinkasserer A.,
Krilis S.
Publication year - 1993
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(93)81771-q
Subject(s) - chinese hamster ovary cell , recombinant dna , glycoprotein , cardiolipin , glycosylation , biochemistry , antibody , chemistry , microbiology and biotechnology , biology , receptor , immunology , phospholipid , membrane , gene
To enable the synthesis of β 2 ‐glycoprotein I mutants we have established a stable Chinese hamster ovary cell line that expresses human β 2 ‐glycoprotein I up to 2.9 μg/10 6 cells/day. Recombinant β 2 ‐glycoprotein I is identical to the purified native protein with respect to cofactor activity revealed in a modified anti‐cardiolipin ELISA. Autoimmune type anti‐cardiolipin antibody requires recombinant β 2 ‐glycoprotein I in a dose‐dependent manner to bind cardiolipin whilst binding of infectious type antibody is inhibited. The purified recombinant β 2 ‐glycoprotein I in serum free medium exists as two oligosaccharide species which upon deglycosylation have identical apparent molecular weight to the deglycosylated native protein.