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. Author manuscript; available in PMC: 2009 Mar 1.

Published in final edited form as: Biochim Biophys Acta. 2008 Jan 12;1782(3):163–168. doi: 10.1016/j.bbadis.2008.01.001

Fig. 2 — Effect of hydrophobic amino acids in the fifth domain of rβ₂GPI at positions 313–316 on its ability to bind to rHBsAg and CL. Four hydrophobic amino acids at positions 313–316 were mutated to neutral amino acids (Trp316Ser, Phe315Ser, Ala314Ser and Leu313Gly) and expressed in COS-1 cells. The secreted rβ₂GPI forms were quantitated by capture ELISA (■) followed by their binding to rHBsAg ( ) or CL ( ). Results are given as mean ± SD from three independent clones in triplicate (n=9).

Inline graphic — Effect of hydrophobic amino acids in the fifth domain of rβ₂GPI at positions 313–316 on its ability to bind to rHBsAg and CL. Four hydrophobic amino acids at positions 313–316 were mutated to neutral amino acids (Trp316Ser, Phe315Ser, Ala314Ser and Leu313Gly) and expressed in COS-1 cells. The secreted rβ₂GPI forms were quantitated by capture ELISA (■) followed by their binding to rHBsAg ( ) or CL ( ). Results are given as mean ± SD from three independent clones in triplicate (n=9).