{"count":839,"next":"http://glycodata.org/api/gdd/glyco-properties/?format=json&page=2","previous":null,"results":[{"id":1,"dataset":"carbohydrate","entity":"methyl alpha-D-mannopyranoside","entity_group":"","entity_class":"glycoside","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"122","unit":"µM","value_reported":"122","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs Concanavalin A, isothermal titration calorimetry (ITC), value from Mandal, Kishore & Brewer (Biochemistry 1994, 33:1149-1156); Ka = 0.82 x 10^4 M^-1","conditions":"Kd vs Concanavalin A, isothermal titration calorimetry (ITC), value from Mandal, Kishore & Brewer (Biochemistry 1994, 33:1149-1156); Ka = 0.82 x 10^4 M^-1","conditions_detail":"Kd vs Concanavalin A, isothermal titration calorimetry (ITC), value from Mandal, Kishore & Brewer (Biochemistry 1994, 33:1149-1156); Ka = 0.82 x 10^4 M^-1 | partner: Concanavalin A | technique: ITC","doi":"10.1016/j.jelechem.2016.09.045","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC5388449/","year":"2016","confidence":"high","comments":"\"The Ka value for methyl alpha-D-mannopyranoside reported in the study was 0.82 x 10^4 (Kd = 122 microM)\"  — Kd value originally from Mandal, Kishore & Brewer 1994 (DOI 10.1021/bi00171a014), quoted in this paper. Monosaccharide, monovalent ITC affinity.  [Bhattarai JK, Tan YH, Pandey B, Fujikawa K, Demchenko AV, Stine KJ, 2016, confidence: high]"},{"id":2,"dataset":"carbohydrate","entity":"monomannoside (Man-C8-SH self-assembled monolayer)","entity_group":"","entity_class":"monosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.07","unit":"µM","value_reported":"70","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated mannoside SAM on gold; reported 70 +/- 19 nM","conditions":"Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated mannoside SAM on gold; reported 70 +/- 19 nM","conditions_detail":"Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated mannoside SAM on gold; reported 70 +/- 19 nM | partner: Concanavalin A | technique: electrochemical impedance spectroscopy","doi":"10.1016/j.jelechem.2016.09.045","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC5388449/","year":"2016","confidence":"high","comments":"\"Man(1-3)Man-C8-SH ... show the comparable Kd of 70 +/- 19, 75 +/- 20 and 81 +/- 31 nM\"  — Surface-immobilized mannoside (multivalent/avidity context), measured by EIS.  [Bhattarai JK, Tan YH, Pandey B, Fujikawa K, Demchenko AV, Stine KJ, 2016, confidence: high]"},{"id":3,"dataset":"carbohydrate","entity":"alpha(1-6)-linked dimannoside (Man(1-6)Man-C8-SH SAM)","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.014","unit":"µM","value_reported":"14","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated dimannoside SAM on gold; reported 14 +/- 4 nM","conditions":"Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated dimannoside SAM on gold; reported 14 +/- 4 nM","conditions_detail":"Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated dimannoside SAM on gold; reported 14 +/- 4 nM | partner: Concanavalin A | technique: electrochemical impedance spectroscopy","doi":"10.1016/j.jelechem.2016.09.045","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC5388449/","year":"2016","confidence":"high","comments":"\"Man(1-6) Man-C8-SH ... show stronger interaction with Con A with Kd of 14 +/- 4 and 30 +/- 5 nM\"  — Surface-immobilized dimannoside, EIS.  [Bhattarai JK, Tan YH, Pandey B, Fujikawa K, Demchenko AV, Stine KJ, 2016, confidence: high]"},{"id":4,"dataset":"carbohydrate","entity":"alpha(1-3,1-6) trimannoside (Man(1-3,1-6)Man-C8-SH SAM)","entity_group":"","entity_class":"oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.03","unit":"µM","value_reported":"30","unit_reported":"nM","method":"Experiment","method_detail":"Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated trimannoside SAM on gold; reported 30 +/- 5 nM","conditions":"Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated trimannoside SAM on gold; reported 30 +/- 5 nM","conditions_detail":"Kd vs Concanavalin A, electrochemical impedance spectroscopy (EIS) on thiolated trimannoside SAM on gold; reported 30 +/- 5 nM | partner: Concanavalin A | technique: electrochemical impedance spectroscopy","doi":"10.1016/j.jelechem.2016.09.045","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC5388449/","year":"2016","confidence":"high","comments":"\"Man(1-3,1-6)Man-C8-SH show stronger interaction with Con A with Kd of 14 +/- 4 and 30 +/- 5 nM\"  — Surface-immobilized core trimannoside, EIS.  [Bhattarai JK, Tan YH, Pandey B, Fujikawa K, Demchenko AV, Stine KJ, 2016, confidence: high]"},{"id":5,"dataset":"carbohydrate","entity":"core trimannoside (methyl 3,6-di-O-(alpha-D-mannopyranosyl)-alpha-D-mannopyranoside)","entity_group":"","entity_class":"oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"2","unit":"µM","value_reported":"2.0","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs Concanavalin A, isothermal titration calorimetry (ITC); O-methylated alpha(1-3,1-6) trimannoside, Ka = 4.90 x 10^5 M^-1 (Mandal & Brewer)","conditions":"Kd vs Concanavalin A, isothermal titration calorimetry (ITC); O-methylated alpha(1-3,1-6) trimannoside, Ka = 4.90 x 10^5 M^-1 (Mandal & Brewer)","conditions_detail":"Kd vs Concanavalin A, isothermal titration calorimetry (ITC); O-methylated alpha(1-3,1-6) trimannoside, Ka = 4.90 x 10^5 M^-1 (Mandal & Brewer) | partner: Concanavalin A | technique: ITC","doi":"10.1021/bi00171a014","source_url":"https://pubmed.ncbi.nlm.nih.gov/8110746/","year":"1994","confidence":"medium","comments":"\"For the O-methylated alpha(1-3,1-6) trimannoside, Ka = 4.90 x 10^5 (Kd = 2.0 microM) was reported, while the O-methylated alpha(1-6)-linked dimannoside showed Ka = 0.81 x 10^4 (Kd = 123 microM)\"  — Core trimannoside is the conserved binding unit of N-linked glycans; ~60-fold higher affinity than methyl mannoside per Mandal & Brewer 1994. Value via search aggregation of the primary ITC paper.  [Mandal DK, Kishore N, Brewer CF, 1994, confidence: medium]"},{"id":6,"dataset":"carbohydrate","entity":"alpha(1-6)-linked dimannoside (O-methylated)","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"123","unit":"µM","value_reported":"123","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs Concanavalin A, isothermal titration calorimetry (ITC); Ka = 0.81 x 10^4 M^-1 (Mandal & Brewer)","conditions":"Kd vs Concanavalin A, isothermal titration calorimetry (ITC); Ka = 0.81 x 10^4 M^-1 (Mandal & Brewer)","conditions_detail":"Kd vs Concanavalin A, isothermal titration calorimetry (ITC); Ka = 0.81 x 10^4 M^-1 (Mandal & Brewer) | partner: Concanavalin A | technique: ITC","doi":"10.1021/bi00171a014","source_url":"https://pubmed.ncbi.nlm.nih.gov/8110746/","year":"1994","confidence":"medium","comments":"\"the O-methylated alpha(1-6)-linked dimannoside showed Ka = 0.81 x 10^4 (Kd = 123 microM)\"  — Value via search aggregation of the primary ITC paper.  [Mandal DK, Kishore N, Brewer CF, 1994, confidence: medium]"},{"id":7,"dataset":"carbohydrate","entity":"lactose","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"89.7","unit":"µM","value_reported":"89.7","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 89.7 +/- 15.8 uM (TFS) / 93.5 +/- 9.1 uM by ITC, 25 C, PBS","conditions":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 89.7 +/- 15.8 uM (TFS) / 93.5 +/- 9.1 uM by ITC, 25 C, PBS","conditions_detail":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 89.7 +/- 15.8 uM (TFS) / 93.5 +/- 9.1 uM by ITC, 25 C, PBS | partner: galectin-3 | technique: intrinsic tryptophan fluorescence | temperature C: 25","doi":"10.1038/s41598-019-47658-8","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/","year":"2019","confidence":"high","comments":"\"followed by lactose (KD, 89.7 +/- 15.8 microM)\"  — Cross-validated with ITC (93.5 +/- 9.1 uM) in same study.  [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]"},{"id":8,"dataset":"carbohydrate","entity":"N-acetyllactosamine (LacNAc)","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"27.9","unit":"µM","value_reported":"27.9","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 27.9 +/- 4.6 uM (TFS) / 24.0 +/- 3.6 uM by ITC, 25 C, PBS","conditions":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 27.9 +/- 4.6 uM (TFS) / 24.0 +/- 3.6 uM by ITC, 25 C, PBS","conditions_detail":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 27.9 +/- 4.6 uM (TFS) / 24.0 +/- 3.6 uM by ITC, 25 C, PBS | partner: galectin-3 | technique: intrinsic tryptophan fluorescence | temperature C: 25","doi":"10.1038/s41598-019-47658-8","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/","year":"2019","confidence":"high","comments":"\"LacNAc emerged as the strongest galectin-3 binding ligand (KD, 27.9 +/- 4.6 microM)\"  — Cross-validated with ITC (24.0 +/- 3.6 uM).  [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]"},{"id":9,"dataset":"carbohydrate","entity":"galactose","entity_group":"","entity_class":"monosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"4700","unit":"µM","value_reported":"4.7","unit_reported":"mM","method":"Experiment","method_detail":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 4.7 +/- 0.3 mM (TFS) / 3.1 +/- 1.1 mM by ITC, 25 C, PBS","conditions":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 4.7 +/- 0.3 mM (TFS) / 3.1 +/- 1.1 mM by ITC, 25 C, PBS","conditions_detail":"Kd vs human galectin-3, intrinsic tryptophan fluorescence spectroscopy (TFS); 4.7 +/- 0.3 mM (TFS) / 3.1 +/- 1.1 mM by ITC, 25 C, PBS | partner: galectin-3 | technique: intrinsic tryptophan fluorescence | temperature C: 25","doi":"10.1038/s41598-019-47658-8","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/","year":"2019","confidence":"high","comments":"\"and galactose (KD, 4.7 +/- 0.3 mM)\"  — Monosaccharide weak binding; cross-validated with ITC (3.1 +/- 1.1 mM).  [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]"},{"id":10,"dataset":"carbohydrate","entity":"N-acetyllactosamine (LacNAc)","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"654.4","unit":"µM","value_reported":"654.4","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs human galectin-2, intrinsic tryptophan fluorescence spectroscopy (TFS); 654.4 +/- 155.4 uM (TFS) / 554.2 +/- 108.0 uM by ITC, 25 C, PBS","conditions":"Kd vs human galectin-2, intrinsic tryptophan fluorescence spectroscopy (TFS); 654.4 +/- 155.4 uM (TFS) / 554.2 +/- 108.0 uM by ITC, 25 C, PBS","conditions_detail":"Kd vs human galectin-2, intrinsic tryptophan fluorescence spectroscopy (TFS); 654.4 +/- 155.4 uM (TFS) / 554.2 +/- 108.0 uM by ITC, 25 C, PBS | partner: galectin-2 | technique: intrinsic tryptophan fluorescence | temperature C: 25","doi":"10.1038/s41598-019-47658-8","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/","year":"2019","confidence":"high","comments":"\"The KD values of LacNAc, lactose and galactose binding to galectin-2 were 654.4 +/- 155.4 microM\"  — Cross-validated with ITC (554.2 +/- 108.0 uM).  [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]"},{"id":11,"dataset":"carbohydrate","entity":"lactose","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"589.3","unit":"µM","value_reported":"589.3","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs human galectin-4 (full-length), intrinsic tryptophan fluorescence spectroscopy (TFS); 589.3 +/- 168.2 uM (TFS) / 738.5 +/- 128.5 uM by ITC, 25 C, PBS","conditions":"Kd vs human galectin-4 (full-length), intrinsic tryptophan fluorescence spectroscopy (TFS); 589.3 +/- 168.2 uM (TFS) / 738.5 +/- 128.5 uM by ITC, 25 C, PBS","conditions_detail":"Kd vs human galectin-4 (full-length), intrinsic tryptophan fluorescence spectroscopy (TFS); 589.3 +/- 168.2 uM (TFS) / 738.5 +/- 128.5 uM by ITC, 25 C, PBS | partner: galectin-4 | technique: intrinsic tryptophan fluorescence | temperature C: 25","doi":"10.1038/s41598-019-47658-8","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC6694196/","year":"2019","confidence":"high","comments":"\"The binding of galectin-4 to lactose (KD, 589.3 +/- 168.2 microM) was stronger than to LacNAc\"  — Cross-validated with ITC (738.5 +/- 128.5 uM). Galectin-4 binds lactose more strongly than LacNAc (unusual).  [Sindrewicz P, Li X, Yates EA, Turnbull JE, Lian LY, Yu LG, 2019, confidence: high]"},{"id":12,"dataset":"carbohydrate","entity":"lactose","entity_group":"","entity_class":"disaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"230","unit":"µM","value_reported":"230","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs galectin-3 carbohydrate recognition domain (Gal3C), ITC and NMR, room temperature","conditions":"Kd vs galectin-3 carbohydrate recognition domain (Gal3C), ITC and NMR, room temperature","conditions_detail":"Kd vs galectin-3 carbohydrate recognition domain (Gal3C), ITC and NMR, room temperature | partner: galectin-3 (Gal3C CRD) | technique: ITC/NMR","doi":"10.1021/bi201459p","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3255464/","year":"2011","confidence":"high","comments":"\"lactose binds to Gal3C with a dissociation constant (Kd) of 230 microM\"  — Same paper also notes 3'-benzamido-LacNAc Kd = 18.2 uM and lactose Kd = 231 uM.  [Saraboji K, Hakansson M, Genheden S, et al., 2011, confidence: high]"},{"id":13,"dataset":"carbohydrate","entity":"3'-benzamido-N-acetyllactosamine","entity_group":"","entity_class":"glycoside","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"18.2","unit":"µM","value_reported":"18.2","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs galectin-3 carbohydrate recognition domain (Gal3C), referenced value, room temperature","conditions":"Kd vs galectin-3 carbohydrate recognition domain (Gal3C), referenced value, room temperature","conditions_detail":"Kd vs galectin-3 carbohydrate recognition domain (Gal3C), referenced value, room temperature | partner: galectin-3 (Gal3C CRD) | technique: ITC","doi":"10.1021/bi201459p","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC3255464/","year":"2011","confidence":"high","comments":"\"affinity of lactose is lower (Kd = 231 microM) than that of 3'-benzamido-N-acetyllactosamine (Kd = 18.2 microM)\"  — Synthetic high-affinity galectin-3 ligand.  [Saraboji K, Hakansson M, Genheden S, et al., 2011, confidence: high]"},{"id":14,"dataset":"carbohydrate","entity":"single N-glycans","entity_group":"","entity_class":"glycan (N-linked)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"50","unit":"µM","value_reported":"50","unit_reported":"uM","method":"Experiment","method_detail":"Approximate Kd vs galectin-1 CRD for single N-glycans (comparison statement)","conditions":"Approximate Kd vs galectin-1 CRD for single N-glycans (comparison statement)","conditions_detail":"Approximate Kd vs galectin-1 CRD for single N-glycans (comparison statement) | partner: galectin-1 | technique: fluorescence anisotropy / comparison","doi":"10.1093/glycob/cwn015","source_url":"https://academic.oup.com/glycob/article/18/5/384/1987867","year":"2008","confidence":"medium","comments":"\"The galectin-1 CRDs bind more weakly to single N-glycans (Kd ~50 microM) compared to galectin-3\"  — Approximate value (~50 uM).  [Cederfur C, Salomonsson E, Nilsson J, et al., 2008, confidence: medium]"},{"id":15,"dataset":"carbohydrate","entity":"human serum glycoproteins (LacNAc-bearing)","entity_group":"","entity_class":"glycan (N-linked)","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"3","unit":"µM","value_reported":"3","unit_reported":"uM","method":"Experiment","method_detail":"Average Kd vs galectin-3, fluorescence anisotropy assay; estimated range 1-5 uM (midpoint 3 uM recorded)","conditions":"Average Kd vs galectin-3, fluorescence anisotropy assay; estimated range 1-5 uM (midpoint 3 uM recorded)","conditions_detail":"Average Kd vs galectin-3, fluorescence anisotropy assay; estimated range 1-5 uM (midpoint 3 uM recorded) | partner: galectin-3 | technique: fluorescence anisotropy","doi":"10.1093/glycob/cwn015","source_url":"https://academic.oup.com/glycob/article/18/5/384/1987867","year":"2008","confidence":"medium","comments":"\"The average affinity of galectin-3 for serum glycoproteins was estimated to correspond to Kd ~1-5 microM\"  — Reported as a range 1-5 uM; midpoint 3 uM recorded for value field. Glycoprotein-level (multivalent) average affinity.  [Cederfur C, Salomonsson E, Nilsson J, et al., 2008, confidence: medium]"},{"id":16,"dataset":"carbohydrate","entity":"L-fucose","entity_group":"","entity_class":"monosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"2.9","unit":"µM","value_reported":"2.9","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC)","conditions":"Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC)","conditions_detail":"Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC) | partner: LecB (PA-IIL), Pseudomonas aeruginosa | technique: ITC","doi":"10.32607/20758251-2015-7-2-29-41","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/","year":"2015","confidence":"high","comments":"\"The dissociation constant of the LecB-L-fucose complex is 2.9 microM\"  — Unusually high monosaccharide affinity due to two calcium ions in the LecB binding site.  [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: high]"},{"id":17,"dataset":"carbohydrate","entity":"methyl-alpha-L-fucoside","entity_group":"","entity_class":"glycoside","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.4","unit":"µM","value_reported":"0.4","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC; ~7-fold lower than free L-fucose","conditions":"Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC; ~7-fold lower than free L-fucose","conditions_detail":"Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC; ~7-fold lower than free L-fucose | partner: LecB (PA-IIL), Pseudomonas aeruginosa | technique: ITC","doi":"10.32607/20758251-2015-7-2-29-41","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/","year":"2015","confidence":"high","comments":"\"the dissociation constant of the LecB-methyl-alpha-L-fucoside complex is sevenfold lower than that of the LecB complex with unmodified L-fucose\"  — ~0.4 uM (sevenfold below the 2.9 uM fucose value).  [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: high]"},{"id":18,"dataset":"carbohydrate","entity":"Lewis a oligosaccharide","entity_group":"","entity_class":"oligosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"0.2","unit":"µM","value_reported":"0.2","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC (210 nM); 0.51 uM by ELLA","conditions":"Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC (210 nM); 0.51 uM by ELLA","conditions_detail":"Kd vs LecB (PA-IIL) from Pseudomonas aeruginosa, ITC (210 nM); 0.51 uM by ELLA | partner: LecB (PA-IIL), Pseudomonas aeruginosa | technique: ITC","doi":"10.32607/20758251-2015-7-2-29-41","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/","year":"2015","confidence":"high","comments":"\"The Kd of the LecB-Lea complex is 210 nM\"  — Lewis a is a natural fucosylated epitope; recorded as 0.2 uM (210 nM).  [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: high]"},{"id":19,"dataset":"carbohydrate","entity":"galactose","entity_group":"","entity_class":"monosaccharide","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"88","unit":"µM","value_reported":"88","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC)","conditions":"Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC)","conditions_detail":"Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, isothermal titration calorimetry (ITC) | partner: LecA (PA-IL), Pseudomonas aeruginosa | technique: ITC","doi":"10.32607/20758251-2015-7-2-29-41","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/","year":"2015","confidence":"high","comments":"\"The dissociation constant of the LecA-galactose complex is 88 microM\"  — LecA (PA-IL) is the galactose-specific lectin of P. aeruginosa.  [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: high]"},{"id":20,"dataset":"carbohydrate","entity":"p-nitrophenyl alpha-D-galactopyranoside","entity_group":"","entity_class":"glycoside","property":"protein binding affinity (Kd)","property_key":"binding_affinity","value":"14.1","unit":"µM","value_reported":"14.1","unit_reported":"uM","method":"Experiment","method_detail":"Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, ITC; reported within 4-15 uM range for aryl galactosides","conditions":"Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, ITC; reported within 4-15 uM range for aryl galactosides","conditions_detail":"Kd vs LecA (PA-IL) from Pseudomonas aeruginosa, ITC; reported within 4-15 uM range for aryl galactosides | partner: LecA (PA-IL), Pseudomonas aeruginosa | technique: ITC","doi":"10.32607/20758251-2015-7-2-29-41","source_url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC4463410/","year":"2015","confidence":"medium","comments":"\"Kd of the complex between LecA and such compounds as phenylgalactopyranoside, p-nitrophenylgalactopyranoside ... is 4-15 microM\"  — Aromatic aglycone enhances affinity over galactose; value within stated 4-15 uM range.  [Grishin AV, Krivozubov MS, Karyagina AS, Gintsburg AL, 2015, confidence: medium]"}]}