A Rapid Electrophoretic Method for the Determination of the Isoenzymes of Serum Lactate Dehydrogenase

1966 ◽  
Vol 12 (5) ◽  
pp. 308-313 ◽  
Author(s):  
Albert W Opher ◽  
Charles S Collier ◽  
Joseph M Miller
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Quantitative Determination ◽  
Serum Lactate ◽  
Serum Lactate Dehydrogenase ◽  
Electrophoretic Method ◽  
The Individual ◽  
Electrophoretic Procedure ◽  
Purple Formazan

Abstract A convenient electrophoretic procedure for the separation and quantitation of lactate dehydrogenase (LDH) isoenzymes is described. The system uses polyacetate Sepraphore III strips.* The areas of activity are shown by incubation with an LDH substrate combined with tetra-nitro-blue-tetrazolium. The reduction of the latter to the purple formazan is quantitatively related to the enzyme activity. Quantitative determination of the individual colored areas is performed by densitometry.

The Automated Determination of NAD-Coupled Enzymes

1966 ◽  
Vol 12 (5) ◽  
pp. 274-281 ◽  
Author(s):  
Stanley Morgenstern ◽  
Richard Flor ◽  
Gerald Kessler, ◽  
Bernard Klein
Keyword(s):  
Lactate Dehydrogenase ◽  
Excellent Agreement ◽  
Nicotinamide Adenine Dinucleotide ◽  
Colorimetric Method ◽  
Serum Lactate ◽  
Serum Lactate Dehydrogenase ◽  
Coupled Enzymes ◽  
Reduced Nicotinamide Adenine Dinucleotide ◽  
Automated Determination

Abstract A precise automated procedure developed for determination of serum lactate dehydrogenase, using the Robot Chemist, measures absorbance of a cuprous-neo-cuproine complex formed by coupled reduction of the cupric-neocuproine reagent with enzymatically generated reduced nicotinamide adenine dinucleotide. Activity values obtained by this method, by the identical automated colorimetric method on the AutoAnalyzer, and by an automated spectrophotometric (34O-mµ) procedure show excellent agreement.

Pyruvate as Substrate in the Determination of Serum Lactate Dehydrogenase Isoenzyme Activity

1974 ◽  
Vol 20 (11) ◽  
pp. 1462-1465 ◽  
Author(s):  
Doris McKenzie ◽  
A R Henderson
Keyword(s):  
Lactate Dehydrogenase ◽  
Serum Lactate ◽  
Serum Lactate Dehydrogenase ◽  
Dehydrogenase Isoenzyme

Abstract Lactate dehydrogenase isoenzyme activity is usually assessed, after the isoenzymes have been separated, by reactions involving lactate as the substrate. We describe a method for their assessment with pyruvate as the substrate. Precision is adequate as compared to the conventional methodology. Application of this type of approach (measurement of a decrease in fluorescence) to determination of other serum isoenzymes is briefly described.

The effect of respiratory diseases on serum lactate dehydrogenase and its isoenzyme patterns in calves

2013 ◽  
Vol 16 (2) ◽  
pp. 211-218 ◽  
Author(s):  
O. Nagy ◽  
Cs. Tóthová ◽  
I. Paulíková ◽  
G. Kováčl ◽  
H. Seidel
Keyword(s):  
Lactate Dehydrogenase ◽  
Respiratory Diseases ◽  
Clinical Signs ◽  
Serum Lactate ◽  
Serum Lactate Dehydrogenase ◽  
Control Group ◽  
Diagnostic Significance ◽  
Organ Systems ◽  
Isoenzyme Patterns

AbstractIn this study we examined the serum activity of lactate dehydrogenase (LDH) and its isoenzyme patterns in 28 calves of a lowland black spotted breed and its crossbreeds at the age of 2-6 months suffering from clinically noticeable manifested respiratory diseases - bronchopneumonia (BRD Group). As a control group we used 35 clinically healthy calves of the same age, breed and nutrition (Healthy Group). The sick calves did not show clinical signs or pathological lesions on other organ systems. The results found in sick calves showed a significantly higher total activity of LDH than in clinically healthy animals (P<0.01). The mean activity of LDH was 2012 U/l in healthy calves and in calves with respiratory diseases 2529 U/l. The differences in all LDH isoenzyme patterns between both groups of animals were significant (P<0.001) and in calves with respiratory diseases are characterized by a marked increase of the LDH 1 fraction and a decrease in the proportion of the other four LDH isoenzymes. Our results differ from those observed and presented in respiratory diseases in human medicine or in sheep. The explanation for the obtained results in calves and the determination of their diagnostic significance needs further studies and investigations using more animals with various severity of clinical signs and pathological changes, including analysis and determination of lactate dehydrogenase isoenzyme patterns in healthy and affected cattle lung tissue.

6.1.1.3 Analytical Bias by Contamination from Hemolysis in Determination of Serum Lactate Dehydrogenase Isoenzyme 1 in Patients with Testis Germ Cell Tumors

1993 ◽  
Vol 98 (3) ◽  
pp. 293-298 ◽  
Author(s):  
Finn Edler von Eyben ◽  
Per Hyltoft Petersen ◽  
Ole Blaabjerg ◽  
Ebbe Lindegaard Madsen ◽  
Bent Nørgaard-Pedersen ◽  
...  
Keyword(s):  
Lactate Dehydrogenase ◽  
Germ Cell ◽  
Germ Cell Tumors ◽  
Serum Lactate ◽  
Serum Lactate Dehydrogenase ◽  
Dehydrogenase Isoenzyme

Amperometric determination of serum lactate dehydrogenase activity using an ADP-modified graphite electrode

2002 ◽  
Vol 457 (2) ◽  
pp. 275-284 ◽  
Author(s):  
Noemı́ de los Santos-Álvarez ◽  
Marı́a Jesús Lobo-Castañón ◽  
Arturo J. Miranda-Ordieres ◽  
Paulino Tuñón-Blanco
Keyword(s):  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Graphite Electrode ◽  
Serum Lactate ◽  
Serum Lactate Dehydrogenase ◽  
Amperometric Determination ◽  
Lactate Dehydrogenase Activity

Spurious Elevation of Apparent Lactate Dehydrogenase Activity Caused by Triamterene

1973 ◽  
Vol 19 (10) ◽  
pp. 1202-1204 ◽  
Author(s):  
T Chainuvati ◽  
U Harinasuta ◽  
H J Zimmerman
Keyword(s):  
Enzyme Activity ◽  
Lactate Dehydrogenase ◽  
Dehydrogenase Activity ◽  
Enzyme Activities ◽  
Physiological Saline ◽  
Serum Lactate ◽  
Normal Serum ◽  
Serum Lactate Dehydrogenase ◽  
Fluorometric Method ◽  
Lactate Dehydrogenase Activity

Abstract Triamterene induced spurious elevations in serum lactate dehydrogenase activity, as assayed by an automated fluorometric method; the enzyme activities were normal when measured spectrophotometrically. Solutions of the drug in normal serum or physiological saline, without addition of substrate or coenzyme, yielded high values for apparent "enzyme" activity by the fluorometric assay.

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