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Title: Variability of intracellular lactate dehydrogenase isoenzymes in single human erythrocytes

Abstract

Trace amounts of enzymes within single human erythrocytes can be quantified by a combination of on-column reaction and capillary electrophoresis. A detection limit of 1.3 x 10[sup [minus]21] mol of LDH was achieved with laser-induced fluorescence by monitoring the product of the enzyme-catalyzed reaction between lactate and NAD[sup +]. Single erythrocyte analysis clearly isolates the major forms of LDH. The variation of total LDH activity in a population of cells from a single individual is large, but the relative activities of the isoenzymes LDH-1 and LDH-2 are fairly constant. This can be explained by the distribution of cell age in the population. A lower enzyme activity is indicative of senescence. The efficient separation of different LDH forms and the high detection sensitivity opens up the possibility of multiple-enzyme assays with a single mammalian cell. 41 refs., 5 figs.

Authors:
;  [1]
  1. Ames Lab., IA (United States) Iowa State Univ., Ames, IA (United States)
Publication Date:
OSTI Identifier:
7070210
DOE Contract Number:  
W-7405-ENG-82
Resource Type:
Journal Article
Journal Name:
Analytical Chemistry (Washington); (United States)
Additional Journal Information:
Journal Volume: 66:7; Journal ID: ISSN 0003-2700
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; 59 BASIC BIOLOGICAL SCIENCES; LACTATES; CHEMICAL REACTIONS; NAD; OXIDOREDUCTASES; ELECTROPHORESIS; CAPILLARIES; CATALYSIS; ERYTHROCYTES; FLUORESCENCE; LASERS; TRACE AMOUNTS; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BLOOD VESSELS; BODY; BODY FLUIDS; CARBOXYLIC ACID SALTS; CARDIOVASCULAR SYSTEM; COENZYMES; ENZYMES; LUMINESCENCE; MATERIALS; NUCLEOTIDES; ORGANIC COMPOUNDS; ORGANS; PROTEINS; 400105* - Separation Procedures; 400400 - Electrochemistry; 550200 - Biochemistry; 550300 - Cytology; 400500 - Photochemistry

Citation Formats

Xue, Q, and Yeung, E S. Variability of intracellular lactate dehydrogenase isoenzymes in single human erythrocytes. United States: N. p., 1994. Web. doi:10.1021/ac00079a036.
Xue, Q, & Yeung, E S. Variability of intracellular lactate dehydrogenase isoenzymes in single human erythrocytes. United States. doi:10.1021/ac00079a036.
Xue, Q, and Yeung, E S. Fri . "Variability of intracellular lactate dehydrogenase isoenzymes in single human erythrocytes". United States. doi:10.1021/ac00079a036.
@article{osti_7070210,
title = {Variability of intracellular lactate dehydrogenase isoenzymes in single human erythrocytes},
author = {Xue, Q and Yeung, E S},
abstractNote = {Trace amounts of enzymes within single human erythrocytes can be quantified by a combination of on-column reaction and capillary electrophoresis. A detection limit of 1.3 x 10[sup [minus]21] mol of LDH was achieved with laser-induced fluorescence by monitoring the product of the enzyme-catalyzed reaction between lactate and NAD[sup +]. Single erythrocyte analysis clearly isolates the major forms of LDH. The variation of total LDH activity in a population of cells from a single individual is large, but the relative activities of the isoenzymes LDH-1 and LDH-2 are fairly constant. This can be explained by the distribution of cell age in the population. A lower enzyme activity is indicative of senescence. The efficient separation of different LDH forms and the high detection sensitivity opens up the possibility of multiple-enzyme assays with a single mammalian cell. 41 refs., 5 figs.},
doi = {10.1021/ac00079a036},
journal = {Analytical Chemistry (Washington); (United States)},
issn = {0003-2700},
number = ,
volume = 66:7,
place = {United States},
year = {1994},
month = {4}
}