Binding of beta 2 glycoprotein I (β 2 GPI) to apoptotic cells plays a key role in the opsonization of apoptotic bodies and the formation of antiphospholipids antibodies. Here, we describe the binding of β 2 GPI to apoptotic cells using β 2 GPI labelled with biotin-hydrazide (β 2 GPI-bh) after oxidation of its glycan chains. Flow cytometry analyses and confocal microscopy showed that β 2 GPI-bh, contrary to native β 2 GPI, bound to apoptotic cells, either permeable or non-permeable to propidium iodide (PI), as did annexin-V–FITC. But, in the absence of divalent ions, β 2 GPI-bh, contrary to annexin V, was still able to bind to apoptotic cells. Binding equilibrium studies, performed on solid-state anionic phospholipids (AnPL), revealed that β 2 GPI-bh had a greater apparent affinity for AnPL than native β 2 GPI. In presence of the anti-β 2 GPI mAb 8C3, the ability of native β 2 GPI to bind to AnPL was increased and binding to apoptotic PI + and PI − CEM cells was observed whereas binding of β 2 GPI-bh was barely affected by the addition of 8C3. However, the 8C3-enhanced ability of native β 2 GPI to bind to AnPL was still weaker than that of β 2 GPI-bh. It is not clear why the oxidation and biotinylation of glycan chains of β 2 GPI increases its affinity for AnPL, but it seems that if such oxidative process occurs naturally, it could participate in enhancing antiphospholipid formation.