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spelling paper:paper_03063623_v31_n3_p441_Caballero2023-06-08T15:31:08Z Reducing sugars trigger δ-aminolevulinic dehydratase inactivation evidence of in vitro aspirin prevention Gerez, Esther Noemí Vázquez, Elba Susana Batlle, Alcira María del Carmen 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. 1998 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03063623_v31_n3_p441_Caballero http://hdl.handle.net/20.500.12110/paper_03063623_v31_n3_p441_Caballero
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection 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
Gerez, Esther Noemí
Vázquez, Elba Susana
Batlle, Alcira María del Carmen
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.
author Gerez, Esther Noemí
Vázquez, Elba Susana
Batlle, Alcira María del Carmen
author_facet Gerez, Esther Noemí
Vázquez, Elba Susana
Batlle, Alcira María del Carmen
author_sort Gerez, Esther Noemí
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
publishDate 1998
url https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_03063623_v31_n3_p441_Caballero
http://hdl.handle.net/20.500.12110/paper_03063623_v31_n3_p441_Caballero
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AT batllealciramariadelcarmen reducingsugarstriggerdaminolevulinicdehydrataseinactivationevidenceofinvitroaspirinprevention
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