Expression of human recombinant β 2 ‐glycoprotein I with anticardiolipin antibody cofactor activity
1993; Wiley; Volume: 326; Issue: 1-3 Linguagem: Inglês
10.1016/0014-5793(93)81771-q
ISSN1873-3468
AutoresS Kouts, C.L. Bunn, Alexander Steinkasserer, Steven A. Krilis,
Tópico(s)Toxin Mechanisms and Immunotoxins
ResumoTo 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.
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