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Potency index, ratio of gallic acid IC50 to test compound IC50 for inhibition of non-enzymatic glycation in hemoglobin (unknown origin) by spectrophotometric analysis
Assay data:2 Tested
SummaryPubMed CitationRelated BioAssays by Target
Inhibition of non-enzymatic glycation in hemoglobin (unknown origin) by spectrophotometric analysis
Assay data:9 Tested
Protein binding to human hemoglobin
Assay data:1 Tested
Binding affinity to hemoglobin in whole blood (unknown origin) at 2 mM incubated for 8 hrs
Assay data:2 Active, 2 Tested
SummaryCompounds, ActivePubMed CitationRelated BioAssays by Target
Binding affinity to hemoglobin in whole blood (unknown origin) at 2 mM incubated for 24 hrs
Assay data:3 Active, 3 Tested
Binding affinity to hemoglobin in whole blood (unknown origin) incubated for 2 hrs
Assay data:5 Active, 5 Tested
Binding affinity to hemoglobin in whole blood (unknown origin) at 2 mM incubated for 2 hrs relative to control
Assay data:5 Tested
Binding affinity to hemoglobin in whole blood (unknown origin) at 1 mM incubated for 2 hrs relative to control
Drug reactivity against betacys93 in hemoglobin (unknown origin) assessed as betacys93-compound adduct formation at 2 mM incubated for 16 hrs by UPLC-MS analysis relative to control
Assay data:4 Tested
Drug reactivity against betacys93 in hemoglobin (unknown origin) assessed as free SH in betacys93 at 2 mM incubated for 16 hrs by UPLC-MS analysis relative to control
Drug reactivity against betacys93 in hemoglobin (unknown origin) assessed as betacys93-compound adduct formation at 2 mM incubated for 2 hrs by UPLC-MS analysis relative to control
Drug reactivity against betacys93 in hemoglobin (unknown origin) assessed as free SH in betacys93 at 2 mM incubated for 2 hrs by UPLC-MS analysis relative to control
Induction of R-state stabilization of Hb betaGlu6Val mutant in sickle disease patient purified HbS/HbA mixture assessed as change from baseline of partial pressure of O2 at which HbS is 50% saturated with O2 at 100 uM preincubated for 45 mins followed by 20 mins oxygenation/deoxygenation cycle by hemoximetry relative to control
Induction of R-state stabilization of Hb betaGlu6Val mutant in sickle disease patient purified HbS/HbA mixture assessed as change from baseline of partial pressure of O2 at which HbS is 50% saturated with O2 at 5 mM preincubated for 45 mins followed by 20 mins oxygenation/deoxygenation cycle by hemoximetry relative to control
Assay data:1 Active, 1 Tested
Induction of R-state stabilization of Hb betaGlu6Val mutant in sickle disease patient purified HbS/HbA mixture assessed as change from baseline of partial pressure of O2 at which HbS is 50% saturated with O2 at 500 uM preincubated for 45 mins followed by oxygenation for 10 mins and subsequent deoxygenation by hemoximetry relative to control
Induction of R-state stabilization of Hb betaGlu6Val mutant in sickle cell disease transfused human whole blood assessed as change from baseline of partial pressure of O2 at which HbS is 50% saturated with O2 at 1 mM preincubated for 45 mins followed by 20 mins oxygenation/deoxygenation cycle by hemoximetry relative to control
Assay data:22 Tested
Induction of R-state stabilization of Hb betaGlu6Val mutant in sickle disease patient purified HbS/HbA mixture assessed as change from baseline of partial pressure of O2 at which HbS is 50% saturated with O2 at 30 uM preincubated for 45 mins followed by oxygenation for 10 mins and subsequent deoxygenation by hemoximetry relative to control
Assay data:42 Tested
Induction of R-state stabilization of Hb in human homozygous sickle red blood cells assessed as change in oxygen pressure at which hemolysates are 50% saturated with oxygen incubated under air for 1 hr followed by 2 hrs incubation under hypoxic condition by oxygen equilibrium curve analysis
Inhibition of sickle hemoglobin polymerization in human homozygous sickle red blood cells assessed as formation of high oxygen affinity schiff-base adducts incubated under air for 1 hr followed by 2 hrs incubation under hypoxic condition by HPLC method
Inhibition of sickle hemoglobin polymerization in human whole blood assessed as formation of high oxygen affinity schiff-base adducts at 2 mM measured after 24 hrs by HPLC method relative to control
Assay data:3 Tested
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