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Titolo:
Selective activity of butyrylcholinesterase in serum by a chemiluminescentassay
Autore:
Yavo, B; Brunetti, IL; da Fonseca, LM; Catalani, LH; Campa, A;
Indirizzi:
Univ Sao Paulo, Fac Ciencias Farmaceut, BR-05508900 Sao Paulo, Brazil UnivSao Paulo Sao Paulo Brazil BR-05508900 BC05508900 Sao Paulo, Brazil Univ Estadual Paulista, Fac Ciencias Farmaceut, BR-14801902 Araraquara, Brazil Univ Estadual Paulista Araraquara Brazil BR-14801902 BCraraquara, Brazil Univ Sao Paulo, Inst Quim, BR-05599970 Sao Paulo, Brazil Univ Sao Paulo Sao Paulo Brazil BR-05599970 BC05599970 Sao Paulo, Brazil
Titolo Testata:
LUMINESCENCE
fascicolo: 5, volume: 16, anno: 2001,
pagine: 299 - 304
SICI:
1522-7235(200109/10)16:5<299:SAOBIS>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOW-DENSITY-LIPOPROTEIN; DIABETES-MELLITUS; PSEUDOCHOLINESTERASE; CHOLINESTERASES; PARAOXONASE; PLASMA;
Keywords:
esterase; butyrylcholinesterase; pseudocholinesterase; horseradish peroxidase; chemiluminescence;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
21
Recensione:
Indirizzi per estratti:
Indirizzo: Campa, A Univ Sao Paulo, Fac Ciencias Farmaceut, CP 66-083, BR-05508900 Sao Paulo, Brazil Univ Sao Paulo CP 66-083 Sao Paulo Brazil BR-05508900 BC, Brazil
Citazione:
B. Yavo et al., "Selective activity of butyrylcholinesterase in serum by a chemiluminescentassay", LUMINESCENC, 16(5), 2001, pp. 299-304

Abstract

In a previous study, we showed that purified commercial esterase activity can be detected in a chemiluminescent assay based on the hydrolysis of 2-methyl-1-propenylbenzoate (MPB) to 2-methyl-1-propenol, which is subsequentlyoxidized by the horseradish peroxidase (HRP)-H2O2 system. The purpose of this study was to verify the applicability of this assay to human serum. Theexistence of an esterase activity capable of hydrolysing MPB is indicated by the fact that the MPB-scruin-HRP-H2O2 System consumes oxygen and emits light. Both signals were abolished by prior serum heat inactivation and werepreserved when serum was stored at less than or equal to4 degreesC. Addition of aliesterase inhibitors, such as fluoride ion and trichlorfon or the cholinesterase inhibitor eserine, totally prevents light emission. The butyrylcholinesterase-specific substrate benzoylcholine causes a delay in both O-2 uptake and light emission, while the specific acetylcholinesterase substrate, acetyl-beta -methylcholine, had practically no effect. Purified butyrylcholinesterase, but not acetylcholinesterase, triggered light emission. The finding that butyryleholinesterase is responsible for the hydrolysis of MPB in serum should serve as the basis for the development of a specific chemiluminescent assay for this enzyme. Copyright (C) 2001 John Wiley & Sons,Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/04/20 alle ore 23:06:12