A　novel　type　of　macroporous　molecularly　imprinted　hybrid　silica　monolithic　column　was　first　developed　for　recognition　of　proteins.　The　macroporous　silica-based　monolithic　skeleton　was　synthesized　in　a　4.6　mm　i.d.　stainless　steel　column　by　a　mild　sol-gel　process　with　methyltrimethoxysilane　(MTMS)　as　a　sole　precursor,　and　then　vinyl　groups　were　introduced　onto　the　surface　of　the　silica　skeleton　by　chemical　modification　of　γ-methacryloxypropyltrimethoxysilane　(γ-MAPS).　Subsequently,　the　molecularly　imprinted　polymer　(MIP)　coating　was　copolymerized　and　anchored　onto　the　surface　of　the　silica　monolith.　Bovine　serum　albumin　(BSA)　and　lysozyme　(Lyz),　which　differ　greatly　in　molecular　size,　isoelectric　point,　and　charge,　were　representatively　selected　for　imprinted　templates　to　evaluate　recognition　property　of　the　hybrid　silica-based　MIP　monolith.　Some　important　factors,　such　as　template-monomer　molar　ratio,　total　monomer　concentration　and　crosslinking　density,　were　systematically　investigated.　Under　the　optimum　conditions,　the　obtained　hybrid　silica-based　MIP　monolith　showed　higher　binding　affinity　for　template　than　its　corresponding　non-imprinted　(NIP)　monolith.　The　imprinted　factor　(IF)　for　BSA　and　Lyz　reached　9.07　and　6.52,　respectively.　Moreover,　the　hybrid　silica-based　MIP　monolith　displayed　favorable　binding　characteristics　for　template　over　competitive　protein.　Compared　with　the　imprinted　silica　beads　for　stationary　phase　and　in　situ　organic　polymer-based　hydrogel　MIP　monolith,　the　hybrid　silica　MIP　monolith　exhibited　higher　recognition,　stability　and　lifetime.　©　2009　Elsevier　B.V.　All　rights　reserved.