دورية أكاديمية
Increased methyl esterification of altered aspartyl residues in erythrocyte membrane proteins in response to oxidative stress.
العنوان: | Increased methyl esterification of altered aspartyl residues in erythrocyte membrane proteins in response to oxidative stress. |
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المؤلفون: | Ingrosso, Diego, D’Angelo, Stefania, di Carlo, Enza, Perna, Alessandra F., Zappia, Vincenzo, Galletti, Patrizia |
المصدر: | European Journal of Biochemistry; Jul2000 Part 2, Vol. 267 Issue 14, p4397-4405, 9p, 4 Diagrams, 1 Chart, 7 Graphs |
مصطلحات موضوعية: | ESTERIFICATION, ERYTHROCYTE membranes |
مستخلص: | Protein-l-isoaspartate (d-aspartate) O-methyltransferase (PCMT; EC 2.1.1.77) catalyses the methyl esterification of the free α-carboxyl group of abnormal l-isoaspartyl residues, which occur spontaneously in protein and peptide substrates as a consequence of molecular ageing. The biological function of this transmethylation reaction is related to the repair or degradation of age-damaged proteins. Methyl ester formation in erythrocyte membrane proteins has also been used as a marker reaction to tag these abnormal residues and to monitor their increase associated with erythrocyte ageing diseases, such as hereditary spherocytosis, or cell stress (thermal or osmotic) conditions. The study shows that levels of l-isoaspartyl residues rise in membrane proteins of human erythrocytes exposed to oxidative stress, induced by t-butyl hydroperoxide or H |
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قاعدة البيانات: | Complementary Index |
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