Determination of enzyme activity in biological fluids by means of electrochemical oxidation of NADH at a modified glassy carbon electrode

L. Bartalits, G. Nagy, E. Pungor

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

This amperometric technique for the determination of enzyme activity is based on detecting a decrease in the concentration of the NADH co-factor of the enzyme reaction. A glassy carbon electrode, modified by adsorption of Mg2+ and NADH, is used to measure the anodic peak current that corresponds to the oxidation of NADH. We found no significant difference between the enzyme activity of lactate dehydrogenase (E.C. 1.1.1.27) preparations as measured by the above amperometric technique and by a spectrophotometric method.

Original languageEnglish
Pages (from-to)1780-1783
Number of pages4
JournalClinical Chemistry
Volume30
Issue number11
Publication statusPublished - 1984

Fingerprint

Electrochemical oxidation
Glassy carbon
Enzyme activity
NAD
Electrodes
Carbon
Fluids
Enzymes
L-Lactate Dehydrogenase
Adsorption
Oxidation

ASJC Scopus subject areas

  • Clinical Biochemistry

Cite this

Determination of enzyme activity in biological fluids by means of electrochemical oxidation of NADH at a modified glassy carbon electrode. / Bartalits, L.; Nagy, G.; Pungor, E.

In: Clinical Chemistry, Vol. 30, No. 11, 1984, p. 1780-1783.

Research output: Contribution to journalArticle

@article{5299397bed434e7da6092ce226547693,
title = "Determination of enzyme activity in biological fluids by means of electrochemical oxidation of NADH at a modified glassy carbon electrode",
abstract = "This amperometric technique for the determination of enzyme activity is based on detecting a decrease in the concentration of the NADH co-factor of the enzyme reaction. A glassy carbon electrode, modified by adsorption of Mg2+ and NADH, is used to measure the anodic peak current that corresponds to the oxidation of NADH. We found no significant difference between the enzyme activity of lactate dehydrogenase (E.C. 1.1.1.27) preparations as measured by the above amperometric technique and by a spectrophotometric method.",
author = "L. Bartalits and G. Nagy and E. Pungor",
year = "1984",
language = "English",
volume = "30",
pages = "1780--1783",
journal = "Clinical Chemistry",
issn = "0009-9147",
publisher = "American Association for Clinical Chemistry Inc.",
number = "11",

}

TY - JOUR

T1 - Determination of enzyme activity in biological fluids by means of electrochemical oxidation of NADH at a modified glassy carbon electrode

AU - Bartalits, L.

AU - Nagy, G.

AU - Pungor, E.

PY - 1984

Y1 - 1984

N2 - This amperometric technique for the determination of enzyme activity is based on detecting a decrease in the concentration of the NADH co-factor of the enzyme reaction. A glassy carbon electrode, modified by adsorption of Mg2+ and NADH, is used to measure the anodic peak current that corresponds to the oxidation of NADH. We found no significant difference between the enzyme activity of lactate dehydrogenase (E.C. 1.1.1.27) preparations as measured by the above amperometric technique and by a spectrophotometric method.

AB - This amperometric technique for the determination of enzyme activity is based on detecting a decrease in the concentration of the NADH co-factor of the enzyme reaction. A glassy carbon electrode, modified by adsorption of Mg2+ and NADH, is used to measure the anodic peak current that corresponds to the oxidation of NADH. We found no significant difference between the enzyme activity of lactate dehydrogenase (E.C. 1.1.1.27) preparations as measured by the above amperometric technique and by a spectrophotometric method.

UR - http://www.scopus.com/inward/record.url?scp=0021699926&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021699926&partnerID=8YFLogxK

M3 - Article

VL - 30

SP - 1780

EP - 1783

JO - Clinical Chemistry

JF - Clinical Chemistry

SN - 0009-9147

IS - 11

ER -