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Titolo:
ASSAY OF PROTEIN-BOUND LIPOIC ACID IN TISSUES BY A NEW ENZYMATIC METHOD
Autore:
AKIBA S; MATSUGO S; PACKER L; KONISHI T;
Indirizzi:
NIIGATA COLL PHARM,DEPT RADIOCHEM BIOPHYS NIIGATA 9502081 JAPAN NIIGATA COLL PHARM,DEPT RADIOCHEM BIOPHYS NIIGATA 9502081 JAPAN TOYAMA UNIV,DEPT CHEM BIOTECHNOL,GOFU KU TOYAMA 9308555 JAPAN UNIV CALIF BERKELEY,DEPT MOL & CELL BIOL BERKELEY CA 94720
Titolo Testata:
Analytical biochemistry
fascicolo: 2, volume: 258, anno: 1998,
pagine: 299 - 304
Fonte:
ISI
Lingua:
ENG
Soggetto:
PYRUVATE-DEHYDROGENASE COMPLEX; DIHYDROLIPOIC ACID; ANTIOXIDANT ACTIVITY; LIPID-PEROXIDATION; BIOLOGICAL SAMPLES; CHROMATOGRAPHY; ELUCIDATION; GLUTATHIONE; LIPOAMIDASE;
Keywords:
LIPOIC ACID; LIPOAMIDE DEHYDROGENASE; ENZYME RECYCLING; GLUTATHIONE DISULFIDE; LIPOYLLYSINE; DIHYDROLIPOIC ACID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
S. Akiba et al., "ASSAY OF PROTEIN-BOUND LIPOIC ACID IN TISSUES BY A NEW ENZYMATIC METHOD", Analytical biochemistry, 258(2), 1998, pp. 299-304

Abstract

A new enzymatic method for the determination of protein-bound lipoic acid was established. Bound lipoyl groups were liberated in the form of lipoyllysine by protease digestion and assayed by lipoamide dehydrogenase (NADH:lipoamide oxidoreductase, EC 1.8.1.4)-mediated NADH oxidation. NADH oxidation was coupled to reduction of the lipoyl disulfide group. Fluorescence kinetics of NADH oxidation were markedly enhanced by the addition of glutathione disulfide, recycling the enzyme-mediatedlipoyl/dihydrolipoyl conversion. In the presence of a large excess ofglutathione disulfide, NADH oxidation follows pseudo-first-order kinetics in terms of lipoyllysine concentration. A good linear correlationis obtained between the oxidation rate and lipoyllysine concentrationup to 5 mu M and the calibration curve indicates that the detection limit could be 100 nM lipoyllysine. The method was applied to protease lysates of bovine, rat, and rabbit tissues to determine lipoyllysine levels. Kidney and liver were found to have the highest content of lipoyllysine in the range of 3.9 to 4.6 nmol/g rat or rabbit wet tissue or11.6 to 13.1 nmol/g bovine acetone powder. (C) 1998 Academic Press.

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Documento generato il 29/09/20 alle ore 18:00:44