{"count":839,"next":"http://glycodata.org/api/gdd/glyco-properties/?format=json&page=34","previous":"http://glycodata.org/api/gdd/glyco-properties/?format=json&page=32","results":[{"id":641,"dataset":"heparin","entity":"heparin dodecasaccharide (two AT-binding pentasaccharides)","entity_group":"","entity_class":"heparin oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.086","unit":"µM","value_reported":"0.086","unit_reported":"µM","method":"Experiment","method_detail":"Kd vs antithrombin (AT) by fluorescence titration at 0.25 M NaCl","conditions":"Kd vs antithrombin (AT) by fluorescence titration at 0.25 M NaCl","conditions_detail":"Kd vs antithrombin (AT) by fluorescence titration at 0.25 M NaCl | partner: antithrombin III | technique: fluorescence | NaCl M: 0.25 | temperature C: 25","doi":"10.1074/jbc.M113.485268","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3764794/","year":"2013","confidence":"high","comments":"\"Binding of the dodecasaccharide to AT was investigated in the presence of 0.1, 0.25, and 0.5 M NaCl yielding Kd values of 0.0099, 0.086, and 1.23 µM, respectively\"  — Dodecasaccharide; 0.25 M NaCl  [Viskov C, Just M, Laux V, Mourier P, Lorenz M, et al., 2013, confidence: high]"},{"id":642,"dataset":"heparin","entity":"heparin dodecasaccharide (two AT-binding pentasaccharides)","entity_group":"","entity_class":"heparin oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"1.23","unit":"µM","value_reported":"1.23","unit_reported":"µM","method":"Experiment","method_detail":"Kd vs antithrombin (AT) by fluorescence titration at 0.5 M NaCl","conditions":"Kd vs antithrombin (AT) by fluorescence titration at 0.5 M NaCl","conditions_detail":"Kd vs antithrombin (AT) by fluorescence titration at 0.5 M NaCl | partner: antithrombin III | technique: fluorescence | NaCl M: 0.5 | temperature C: 25","doi":"10.1074/jbc.M113.485268","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3764794/","year":"2013","confidence":"high","comments":"\"Binding of the dodecasaccharide to AT was investigated in the presence of 0.1, 0.25, and 0.5 M NaCl yielding Kd values of 0.0099, 0.086, and 1.23 µM, respectively\"  — Dodecasaccharide; 0.5 M NaCl  [Viskov C, Just M, Laux V, Mourier P, Lorenz M, et al., 2013, confidence: high]"},{"id":643,"dataset":"heparin","entity":"heparin pentasaccharide (synthetic AT-binding)","entity_group":"","entity_class":"synthetic","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.036","unit":"µM","value_reported":"36","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs antithrombin by stopped-flow / equilibrium protein fluorescence titration","conditions":"Kd vs antithrombin by stopped-flow / equilibrium protein fluorescence titration","conditions_detail":"Kd vs antithrombin by stopped-flow / equilibrium protein fluorescence titration | partner: antithrombin III | technique: fluorescence","doi":"10.1016/S0021-9258(18)42309-5","source_url":"https://www.sciencedirect.com/science/article/pii/S0021925818423095","year":"1992","confidence":"high","comments":"\"pentasaccharide and full-length heparins bound antithrombin with KD values of 36 ± 11 and 10 ± 3 nM, respectively\"  — Classic Olson & Bjork pentasaccharide-AT value  [Olson ST, Björk I, Sheffer R, Craig PA, Shore JD, Choay J, 1992, confidence: high]"},{"id":644,"dataset":"heparin","entity":"heparin (high-affinity, full-length)","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.01","unit":"µM","value_reported":"10","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs antithrombin by stopped-flow / equilibrium protein fluorescence titration","conditions":"Kd vs antithrombin by stopped-flow / equilibrium protein fluorescence titration","conditions_detail":"Kd vs antithrombin by stopped-flow / equilibrium protein fluorescence titration | partner: antithrombin III | technique: fluorescence","doi":"10.1016/S0021-9258(18)42309-5","source_url":"https://www.sciencedirect.com/science/article/pii/S0021925818423095","year":"1992","confidence":"high","comments":"\"pentasaccharide and full-length heparins bound antithrombin with KD values of 36 ± 11 and 10 ± 3 nM, respectively\"  — Full-length high-affinity heparin vs AT  [Olson ST, Björk I, Sheffer R, Craig PA, Shore JD, Choay J, 1992, confidence: high]"},{"id":645,"dataset":"heparin","entity":"heparin pentasaccharide (synthetic AT-binding)","entity_group":"","entity_class":"synthetic","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.043","unit":"µM","value_reported":"43","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs wild-type antithrombin (NRE YEH) by fluorescence titration, I 0.35 phosphate buffer pH 7.4, 25 C","conditions":"Kd vs wild-type antithrombin (NRE YEH) by fluorescence titration, I 0.35 phosphate buffer pH 7.4, 25 C","conditions_detail":"Kd vs wild-type antithrombin (NRE YEH) by fluorescence titration, I 0.35 phosphate buffer pH 7.4, 25 C | partner: antithrombin III (wild-type) | technique: fluorescence | ionic strength I: 0.35 | pH: 7.4 | temperature C: 25","doi":"10.1074/jbc.M114.611707","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4256340/","year":"2014","confidence":"high","comments":"\"Equilibrium dissociation constants (KD) ... associated with heparin pentasaccharide binding ... were measured in I 0.35 phosphate buffer, pH 7.4, at 25 °C by fluorescence titrations (NRE YEH (WT) KD = 43 ± 3 nM)\"  — WT AT reference value at I 0.35 (deliberately weakened to allow accurate Kd)  [Izaguirre G, Aguila S, Qi L, Swanson R, Roth R, et al., 2014, confidence: high]"},{"id":646,"dataset":"heparin","entity":"heparin pentasaccharide (synthetic AT-binding)","entity_group":"","entity_class":"synthetic","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.331","unit":"µM","value_reported":"331","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs antithrombin His319 exosite mutant (NRE YEA) by fluorescence titration, I 0.35 pH 7.4, 25 C","conditions":"Kd vs antithrombin His319 exosite mutant (NRE YEA) by fluorescence titration, I 0.35 pH 7.4, 25 C","conditions_detail":"Kd vs antithrombin His319 exosite mutant (NRE YEA) by fluorescence titration, I 0.35 pH 7.4, 25 C | partner: antithrombin III (His319 mutant) | technique: fluorescence | ionic strength I: 0.35 | pH: 7.4 | temperature C: 25","doi":"10.1074/jbc.M114.611707","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4256340/","year":"2014","confidence":"high","comments":"\"NRE YEA ... KD = 331 ± 20 nM\"  — Exosite mutant reduces pentasaccharide affinity ~8-fold vs WT  [Izaguirre G, Aguila S, Qi L, Swanson R, Roth R, et al., 2014, confidence: high]"},{"id":647,"dataset":"heparin","entity":"heparin","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.0036","unit":"µM","value_reported":"3.6","unit_reported":"nM","method":"Experiment","method_detail":"Kd (KD) vs antithrombin by SPR; ka = 1.2e5 1/Ms, kd = 4.4e-4 1/s","conditions":"Kd (KD) vs antithrombin by SPR; ka = 1.2e5 1/Ms, kd = 4.4e-4 1/s","conditions_detail":"Kd (KD) vs antithrombin by SPR; ka = 1.2e5 1/Ms, kd = 4.4e-4 1/s | partner: antithrombin III | technique: SPR","doi":"10.3389/fmolb.2022.954752","source_url":"https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2022.954752/full","year":"2022","confidence":"high","comments":"\"AT-heparin interaction: ka = 1.2 × 105 1/Ms, kd = 4.4 × 10–4 1/s, and KD = 3.6 nM\"  — SPR heparin-AT KD  [Zhang W, Jin W, Pomin VH, Zhang F, Linhardt RJ, 2022, confidence: high]"},{"id":648,"dataset":"heparin","entity":"heparin","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.0012","unit":"µM","value_reported":"1.2","unit_reported":"nM","method":"Experiment","method_detail":"Kd (KD) vs platelet factor 4 (PF4) by SPR; ka = 9.6e4 1/Ms, kd = 1.1e-4 1/s","conditions":"Kd (KD) vs platelet factor 4 (PF4) by SPR; ka = 9.6e4 1/Ms, kd = 1.1e-4 1/s","conditions_detail":"Kd (KD) vs platelet factor 4 (PF4) by SPR; ka = 9.6e4 1/Ms, kd = 1.1e-4 1/s | partner: platelet factor 4 (PF4) | technique: SPR","doi":"10.3389/fmolb.2022.954752","source_url":"https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2022.954752/full","year":"2022","confidence":"high","comments":"\"PF4-heparin interaction: ka = 9.6 × 104 1/Ms, kd = 1.1 × 10–4 1/s, and KD = 1.2 nM\"  — SPR heparin-PF4 KD  [Zhang W, Jin W, Pomin VH, Zhang F, Linhardt RJ, 2022, confidence: high]"},{"id":649,"dataset":"heparin","entity":"heparin (unfractionated)","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.0552","unit":"µM","value_reported":"55.2","unit_reported":"nM","method":"Experiment","method_detail":"KD vs platelet factor 4 (PF4) by biolayer interferometry (BLI); biotinylated heparin on streptavidin sensors, PF4 in solution","conditions":"KD vs platelet factor 4 (PF4) by biolayer interferometry (BLI); biotinylated heparin on streptavidin sensors, PF4 in solution","conditions_detail":"KD vs platelet factor 4 (PF4) by biolayer interferometry (BLI); biotinylated heparin on streptavidin sensors, PF4 in solution | partner: platelet factor 4 (PF4) | technique: biolayer interferometry (BLI)","doi":"10.3389/fmolb.2022.966754","source_url":"https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2022.966754/full","year":"2022","confidence":"high","comments":"\"KD for the PF4-HP interaction was 55.2 (±1.42) nM, respectively\"  — BLI; HP = unfractionated heparin  [Chen Z, Bhagwat N, Zhang F, Pomin VH, Wang C, et al., 2022, confidence: high]"},{"id":650,"dataset":"heparin","entity":"heparin (high-affinity, HO16)","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.05","unit":"µM","value_reported":"0.05","unit_reported":"µM","method":"Experiment","method_detail":"Kd vs platelet factor 4 (PF4) by isothermal titration calorimetry (ITC); exothermic binding","conditions":"Kd vs platelet factor 4 (PF4) by isothermal titration calorimetry (ITC); exothermic binding","conditions_detail":"Kd vs platelet factor 4 (PF4) by isothermal titration calorimetry (ITC); exothermic binding | partner: platelet factor 4 (PF4) | technique: ITC","doi":"10.3389/fmolb.2022.954752","source_url":"https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2022.954752/full","year":"2022","confidence":"medium","comments":"\"Kd ... for PF4 complexes with different heparins: HO16 heparin (0.05 µM), LMWH (0.09 µM), and UFH (0.14 µM)\"  — ITC PF4 vs high-affinity HO16 heparin; values from search summary of this paper  [Zhang W, Jin W, Pomin VH, Zhang F, Linhardt RJ, 2022, confidence: medium]"},{"id":651,"dataset":"heparin","entity":"LMWH","entity_group":"","entity_class":"LMWH","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.09","unit":"µM","value_reported":"0.09","unit_reported":"µM","method":"Experiment","method_detail":"Kd vs platelet factor 4 (PF4) by isothermal titration calorimetry (ITC)","conditions":"Kd vs platelet factor 4 (PF4) by isothermal titration calorimetry (ITC)","conditions_detail":"Kd vs platelet factor 4 (PF4) by isothermal titration calorimetry (ITC) | partner: platelet factor 4 (PF4) | technique: ITC","doi":"10.3389/fmolb.2022.954752","source_url":"https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2022.954752/full","year":"2022","confidence":"medium","comments":"\"Kd ... for PF4 complexes with different heparins: HO16 heparin (0.05 µM), LMWH (0.09 µM), and UFH (0.14 µM)\"  — ITC PF4 vs LMWH  [Zhang W, Jin W, Pomin VH, Zhang F, Linhardt RJ, 2022, confidence: medium]"},{"id":652,"dataset":"heparin","entity":"heparin (UFH)","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.14","unit":"µM","value_reported":"0.14","unit_reported":"µM","method":"Experiment","method_detail":"Kd vs platelet factor 4 (PF4) by isothermal titration calorimetry (ITC)","conditions":"Kd vs platelet factor 4 (PF4) by isothermal titration calorimetry (ITC)","conditions_detail":"Kd vs platelet factor 4 (PF4) by isothermal titration calorimetry (ITC) | partner: platelet factor 4 (PF4) | technique: ITC","doi":"10.3389/fmolb.2022.954752","source_url":"https://www.frontiersin.org/journals/molecular-biosciences/articles/10.3389/fmolb.2022.954752/full","year":"2022","confidence":"medium","comments":"\"Kd ... for PF4 complexes with different heparins: HO16 heparin (0.05 µM), LMWH (0.09 µM), and UFH (0.14 µM)\"  — ITC PF4 vs UFH  [Zhang W, Jin W, Pomin VH, Zhang F, Linhardt RJ, 2022, confidence: medium]"},{"id":653,"dataset":"heparin","entity":"heparin","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.0006","unit":"µM","value_reported":"0.64","unit_reported":"nM","method":"Experiment","method_detail":"Kd (KD = 6.4e-10 M) vs wild-type recombinant antithrombin by SPR on immobilized heparin","conditions":"Kd (KD = 6.4e-10 M) vs wild-type recombinant antithrombin by SPR on immobilized heparin","conditions_detail":"Kd (KD = 6.4e-10 M) vs wild-type recombinant antithrombin by SPR on immobilized heparin | partner: antithrombin III (wild-type) | technique: SPR","doi":"10.3390/biom11040544","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC8068293/","year":"2021","confidence":"high","comments":"\"strongest AT-heparin binding was observed ... KD = 6.4 × 10−10 M\"  — Wild-type AT-heparin SPR; reported as 6.4e-10 M  [Gindele R, Olah Z, Ilonczai P, Speker M, Udvari A, et al., 2021, confidence: high]"},{"id":654,"dataset":"heparin","entity":"heparin","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.0215","unit":"µM","value_reported":"21.5","unit_reported":"nM","method":"Experiment","method_detail":"Kd (KD = 2.15e-8 M; KA = 1.62e8 1/M) vs antithrombin Budapest 3 mutant by SPR","conditions":"Kd (KD = 2.15e-8 M; KA = 1.62e8 1/M) vs antithrombin Budapest 3 mutant by SPR","conditions_detail":"Kd (KD = 2.15e-8 M; KA = 1.62e8 1/M) vs antithrombin Budapest 3 mutant by SPR | partner: antithrombin III (Budapest 3 mutant) | technique: SPR","doi":"10.3390/biom11040544","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC8068293/","year":"2021","confidence":"high","comments":"\"KD = 2.15 × 10−8 M, KA = 1.62 × 108 1/M\"  — AT Budapest 3 (Leu131Phe) mutant; ~33-fold weaker than WT  [Gindele R, Olah Z, Ilonczai P, Speker M, Udvari A, et al., 2021, confidence: high]"},{"id":655,"dataset":"heparin","entity":"heparin","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.764","unit":"µM","value_reported":"764","unit_reported":"nM","method":"Experiment","method_detail":"Kd (KD = 7.64e-7 M; KA = 2.40e6 1/M) vs antithrombin Basel mutant by SPR","conditions":"Kd (KD = 7.64e-7 M; KA = 2.40e6 1/M) vs antithrombin Basel mutant by SPR","conditions_detail":"Kd (KD = 7.64e-7 M; KA = 2.40e6 1/M) vs antithrombin Basel mutant by SPR | partner: antithrombin III (Basel mutant) | technique: SPR","doi":"10.3390/biom11040544","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC8068293/","year":"2021","confidence":"high","comments":"\"KD = 7.64 × 10−7 M and, KA = 2.40 × 106 1/M\"  — AT Basel mutant; heparin-binding-site defect  [Gindele R, Olah Z, Ilonczai P, Speker M, Udvari A, et al., 2021, confidence: high]"},{"id":656,"dataset":"heparin","entity":"heparin","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"1.08","unit":"µM","value_reported":"1.08","unit_reported":"µM","method":"Experiment","method_detail":"Kd (KD = 1.08e-6 M) vs antithrombin Padua mutant by SPR; weakest interaction","conditions":"Kd (KD = 1.08e-6 M) vs antithrombin Padua mutant by SPR; weakest interaction","conditions_detail":"Kd (KD = 1.08e-6 M) vs antithrombin Padua mutant by SPR; weakest interaction | partner: antithrombin III (Padua mutant) | technique: SPR","doi":"10.3390/biom11040544","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC8068293/","year":"2021","confidence":"high","comments":"\"AT Padua had the weakest interaction ... KD = 1.08 × 10−6 M\"  — AT Padua (Arg47His) mutant; weakest heparin binding  [Gindele R, Olah Z, Ilonczai P, Speker M, Udvari A, et al., 2021, confidence: high]"},{"id":657,"dataset":"heparin","entity":"heparin","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.039","unit":"µM","value_reported":"39","unit_reported":"nM","method":"Experiment","method_detail":"KD vs FGF-2 by surface plasmon resonance (SPR), heparin immobilized on sensor chip","conditions":"KD vs FGF-2 by surface plasmon resonance (SPR), heparin immobilized on sensor chip","conditions_detail":"KD vs FGF-2 by surface plasmon resonance (SPR), heparin immobilized on sensor chip | partner: fibroblast growth factor 2 (FGF-2) | technique: SPR","doi":"10.1016/j.ab.2008.10.012","source_url":"https://www.researchgate.net/publication/23498459_A_surface_plasmon_resonance-based_solution_affinity_assay_for_heparan_sulfate-binding_proteins","year":"2009","confidence":"medium","comments":"\"FGF-2 binds to heparin with a dissociation constant (KD) of 39 nM, as measured by surface plasmon resonance\"  — FGF-2 / heparin SPR; value via web search summary of this SPR solution-affinity assay paper  [Zhang F, Liang X, Pu D, George KI, Holland PJ, Walsh ST, Linhardt RJ, 2009, confidence: medium]"},{"id":658,"dataset":"heparin","entity":"heparin (immobilized)","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.08","unit":"µM","value_reported":"80","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs VEGF165 by SPR, 1:1 Langmuir fit (Table 1)","conditions":"Kd vs VEGF165 by SPR, 1:1 Langmuir fit (Table 1)","conditions_detail":"Kd vs VEGF165 by SPR, 1:1 Langmuir fit (Table 1) | partner: VEGF165 | technique: SPR","doi":"10.1042/BSR20110077","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3190640/","year":"2012","confidence":"high","comments":"\"Both sets of sensorgrams of VEGF55-heparin and VEGF165-heparin interaction fit well with the 1:1 Langmuir binding model (VEGF165-heparin Kd 80 nM)\"  — VEGF165 vs immobilized heparin; Table 1  [Zhao W, McCallum SA, Xiao Z, Zhang F, Linhardt RJ, 2012, confidence: high]"},{"id":659,"dataset":"heparin","entity":"heparin (immobilized)","entity_group":"","entity_class":"heparin (UFH)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.197","unit":"µM","value_reported":"197","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs VEGF55 by SPR, 1:1 Langmuir fit (Table 1)","conditions":"Kd vs VEGF55 by SPR, 1:1 Langmuir fit (Table 1)","conditions_detail":"Kd vs VEGF55 by SPR, 1:1 Langmuir fit (Table 1) | partner: VEGF55 | technique: SPR","doi":"10.1042/BSR20110077","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3190640/","year":"2012","confidence":"high","comments":"\"VEGF55-heparin ... Kd 197 nM (1:1 Langmuir binding model)\"  — VEGF55 (exon-7-deleted) vs immobilized heparin; Table 1  [Zhao W, McCallum SA, Xiao Z, Zhang F, Linhardt RJ, 2012, confidence: high]"},{"id":660,"dataset":"heparin","entity":"heparin octasaccharide (dp8, trisulfated repeats)","entity_group":"","entity_class":"heparin oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"5.5","unit":"µM","value_reported":"5.5","unit_reported":"µM","method":"Experiment","method_detail":"Kd vs VEGF165 by SPR solution affinity assay (oligosaccharide 8b)","conditions":"Kd vs VEGF165 by SPR solution affinity assay (oligosaccharide 8b)","conditions_detail":"Kd vs VEGF165 by SPR solution affinity assay (oligosaccharide 8b) | partner: VEGF165 | technique: SPR","doi":"10.1042/BSR20110077","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3190640/","year":"2012","confidence":"high","comments":"\"8b (octasaccharide) ... VEGF165 5.5 ± 0.7 µM (SPR solution affinity)\"  — Octasaccharide is minimum size to efficiently bind VEGF; Table 2  [Zhao W, McCallum SA, Xiao Z, Zhang F, Linhardt RJ, 2012, confidence: high]"}]}