Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention
The effect of in vitro glycation on δ-aminolevulinic dehydratase (ALA-D) under several experimental conditions was investigated. When preincubated with 500 mM glucose at 37°C for 20 hr, ALA-D was 80% inactivated and glycated hemoglobin levels were increased more than fourfold.Thiobarbituric acid spe...
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todo:paper_03063623_v31_n3_p441_Caballero2023-10-03T15:22:17Z Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention Caballero, F.A. Gerez, E.N. Polo, C.F. Vazquez, E.S. Del C. Batlle, A.M. δ-aminolevulinic dehydratase Acetyl salicylic acid Carbohydrates Enzyme inactivation Glycated hemoglobin Glycation Lipid peroxidation acetylsalicylic acid carbohydrate glycosylated hemoglobin porphobilinogen synthase thiobarbituric acid article enzyme activity enzyme inactivation erythrocyte human human cell lipid peroxidation priority journal protein glycosylation temperature Aspirin Carbohydrate Metabolism Carbohydrates Glucose Glycosylation Hemoglobin A, Glycosylated Humans Lipid Peroxidation Porphobilinogen Synthase Temperature Time Factors The effect of in vitro glycation on δ-aminolevulinic dehydratase (ALA-D) under several experimental conditions was investigated. When preincubated with 500 mM glucose at 37°C for 20 hr, ALA-D was 80% inactivated and glycated hemoglobin levels were increased more than fourfold.Thiobarbituric acid species were not modified during glycation; therefore ALA-D inactivation cannot be attributed to glucose autoxidation.Acetyl salicylic acid was effective in preventing both hemoglobin glycation and ALA-D inactivation by glucose.A method has been developed for measuring protein glycation in vitro, in a crude preparation of red blood cells, which can also be applied to sugars other than glucose. Copyright (C) 1998 Elsevier Science Inc. Fil:Gerez, E.N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Vazquez, E.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03063623_v31_n3_p441_Caballero |
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Universidad de Buenos Aires |
| institution_str |
I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
δ-aminolevulinic dehydratase Acetyl salicylic acid Carbohydrates Enzyme inactivation Glycated hemoglobin Glycation Lipid peroxidation acetylsalicylic acid carbohydrate glycosylated hemoglobin porphobilinogen synthase thiobarbituric acid article enzyme activity enzyme inactivation erythrocyte human human cell lipid peroxidation priority journal protein glycosylation temperature Aspirin Carbohydrate Metabolism Carbohydrates Glucose Glycosylation Hemoglobin A, Glycosylated Humans Lipid Peroxidation Porphobilinogen Synthase Temperature Time Factors |
| spellingShingle |
δ-aminolevulinic dehydratase Acetyl salicylic acid Carbohydrates Enzyme inactivation Glycated hemoglobin Glycation Lipid peroxidation acetylsalicylic acid carbohydrate glycosylated hemoglobin porphobilinogen synthase thiobarbituric acid article enzyme activity enzyme inactivation erythrocyte human human cell lipid peroxidation priority journal protein glycosylation temperature Aspirin Carbohydrate Metabolism Carbohydrates Glucose Glycosylation Hemoglobin A, Glycosylated Humans Lipid Peroxidation Porphobilinogen Synthase Temperature Time Factors Caballero, F.A. Gerez, E.N. Polo, C.F. Vazquez, E.S. Del C. Batlle, A.M. Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention |
| topic_facet |
δ-aminolevulinic dehydratase Acetyl salicylic acid Carbohydrates Enzyme inactivation Glycated hemoglobin Glycation Lipid peroxidation acetylsalicylic acid carbohydrate glycosylated hemoglobin porphobilinogen synthase thiobarbituric acid article enzyme activity enzyme inactivation erythrocyte human human cell lipid peroxidation priority journal protein glycosylation temperature Aspirin Carbohydrate Metabolism Carbohydrates Glucose Glycosylation Hemoglobin A, Glycosylated Humans Lipid Peroxidation Porphobilinogen Synthase Temperature Time Factors |
| description |
The effect of in vitro glycation on δ-aminolevulinic dehydratase (ALA-D) under several experimental conditions was investigated. When preincubated with 500 mM glucose at 37°C for 20 hr, ALA-D was 80% inactivated and glycated hemoglobin levels were increased more than fourfold.Thiobarbituric acid species were not modified during glycation; therefore ALA-D inactivation cannot be attributed to glucose autoxidation.Acetyl salicylic acid was effective in preventing both hemoglobin glycation and ALA-D inactivation by glucose.A method has been developed for measuring protein glycation in vitro, in a crude preparation of red blood cells, which can also be applied to sugars other than glucose. Copyright (C) 1998 Elsevier Science Inc. |
| format |
JOUR |
| author |
Caballero, F.A. Gerez, E.N. Polo, C.F. Vazquez, E.S. Del C. Batlle, A.M. |
| author_facet |
Caballero, F.A. Gerez, E.N. Polo, C.F. Vazquez, E.S. Del C. Batlle, A.M. |
| author_sort |
Caballero, F.A. |
| title |
Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention |
| title_short |
Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention |
| title_full |
Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention |
| title_fullStr |
Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention |
| title_full_unstemmed |
Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention |
| title_sort |
reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention |
| url |
http://hdl.handle.net/20.500.12110/paper_03063623_v31_n3_p441_Caballero |
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1807315658685284352 |