A　macroporous　boronate　affinity　monolithic　column　was　prepared　and　applied　to　specifically　capture　glycoproteins　using　metal-organic　gels　(MOGs)　as　a　porogenic　template.　This　newly　explored　application　of　MOGs　has　proven　to　be　a　more　convenient　method　for　the　formation　of　macropores　in　contrast　to　traditional　porogenic　methods.　The　poly　(3-acrylamidophenylboronic　acid-co-ethylene　dimethacrylate)　monolithic　columns　were　synthesized　in　stainless　columns　by　in　situ　polymerization.　To　fabricate　the　macroporous　formation　with　a　uniformed　open-channel　network,　the　preparation　conditions,　such　as　reaction　temperature,　the　concentration　of　the　MOGs　and　the　ratio　of　monomers　were　systematically　investigated.　The　prepared　macroporous　monoliths　were　characterized　by　scanning　electron　microscope　(SEM)　and　mercury　intrusion　porosimetry.　Furthermore,　horseradish　peroxidase　(HRP)　and　transferrin　(TF)　were　chosen　as　test　glycoproteins,　and　the　chromatographic　analysis　demonstrated　that　the　macroporous　boronate　affinity　monoliths　exhibited　a　higher　selectivity　and　better　dynamic　binding　capacity　toward　glycoproteins　compared　with　non-glycoproteins.　The　resulted　affinity　monolithic　column　was　successfully　employed　to　specifically　capture　TF　from　a　bovine　serum　sample.　©　2011　Elsevier　B.V.