Glyco Property List
Pooled literature properties (glycanDB). Optional filters: ?dataset=uv_vis&property_key=...
GET /api/gdd/glyco-properties/?format=api&page=33
{ "count": 839, "next": "http://glycodata.org/api/gdd/glyco-properties/?format=api&page=34", "previous": "http://glycodata.org/api/gdd/glyco-properties/?format=api&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]" } ] }