A quantitative method for the estimation of tissue lactate dehydrogenase isoenzymes on cellulose acetate

1968 ◽  
Vol 19 (1) ◽  
pp. 139-145 ◽  
Author(s):  
B.H. Stagg ◽  
G.A. Whyley
Keyword(s):  
Lactate Dehydrogenase ◽  
Cellulose Acetate ◽  
Quantitative Method ◽  
Lactate Dehydrogenase Isoenzymes

Diagnosis of hemolytic disease by electrophoresis of erythrocyte lactate dehydrogenase isoenzymes on cellulose acetate or Agarose.

1981 ◽  
Vol 27 (8) ◽  
pp. 1453-1455 ◽  
Author(s):  
F Van Lente ◽  
A Marchand ◽  
R S Galen
Keyword(s):  
Lactate Dehydrogenase ◽  
Cellulose Acetate ◽  
Predictive Value ◽  
In Vitro Models ◽  
Hemolytic Disease ◽  
Cellulose Acetate Electrophoresis ◽  
Lactate Dehydrogenase Isoenzymes

Abstract We determined the LD-1/LD-2 isoenzyme ratio in hemolysates of erythrocytes by electrophoresis on cellulose acetate and on agarose. A ratio exceeding 1.0 was found with the former but not the latter. Results were similar for in vitro models of hemolytic disorders. Using cellulose acetate electrophoresis, we determined the predictive value of data on total LD activity and of the LD-1/LD-2 ratio in diagnosis of hemolytic disease in 100 patients. The sensitivity of the "flipped" LD-1/LD-2 ratio was only 58%, the specificity was 93%, and the predictive value was 74% for diagnosis of hemolytic disease. A normal total LD activity is highly predictive (92%) for ruling at the presence of hemolytic disease.

Improved column method for separating lactate dehydrogenase isoenzymes 1 and 2.

1978 ◽  
Vol 24 (3) ◽  
pp. 480-482 ◽  
Author(s):  
D W Mercer
Keyword(s):  
Myocardial Infarction ◽  
Acute Myocardial Infarction ◽  
Creatine Kinase ◽  
Heart Disease ◽  
Lactate Dehydrogenase ◽  
Sodium Chloride ◽  
Lactate Dehydrogenase Activity ◽  
Column Method ◽  
Creatine Kinase Mb ◽  
Lactate Dehydrogenase Isoenzymes

Abstract Lactate dehydrogenase (LD) isoenzymes 1 and 2 in human serum were separated on a column of diethylaminoethyl-Sephadex. Samples layered on mini-columns were eluted with buffered sodium chloride (100, 150, and 200 mmol/liter). Lactate dehydrogenase activity in column effluents was measured by the Wacker method, and their isoenzyme content was evaluated by electrophoresis on polyacrylamide gel. Results for column-fractionated LD-1 and LD-2 were expressed in two ways: LD-1/LD-2 ratios and total LD-1 + LD-2 activities. The former is a more specific indicator of myocardial infarction than the latter. Sera from 10 patients with acute myocardial infarction (increased creatine kinease isoenzyme MB activity) exhibited ratios in the range of 0.92 to 1.56, ratios for 10 patients without heart disease (normal creatine kinase MB) ranged from 0.33 to 0.69.

The Identification of the Enzymes That Catalyse the Oxidation of Glyoxylate to Oxalate in the 100 000 g Supernatant Fraction of Human Hyperoxaluric and Control Liver and Heart Tissue

1973 ◽  
Vol 44 (3) ◽  
pp. 227-241 ◽  
Author(s):  
Dorothy A. Gibbs ◽  
R. W. E. Watts
Keyword(s):  
Lactate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Liver Tissue ◽  
Primary Hyperoxaluria ◽  
Heart Tissue ◽  
Supernatant Fraction ◽  
Glycollate Oxidase ◽  
And Control ◽  
Oxalate Synthesis ◽  
Lactate Dehydrogenase Isoenzymes

1. The enzymic oxidation of glyoxylate to oxalate in the soluble (100 000 g supernatant) fraction of liver and heart tissue from a patient with primary hyperoxaluria and from a non-hyperoxaluric subject have been studied. 2. An oxidized nicotinamide—adenine dinucleotide (NAD+)-dependent and a non-NAD+-dependent oxidation of glyoxylate to oxalate were observed in the liver tissue from both sources. 3. Evidence is presented that lactate dehydrogenase has a major role in catalysing the reaction in both of the tissues studied. The non-NAD+-dependent oxidations which are catalysed by xanthine oxidase and glycollate oxidase in the liver are relatively unimportant, and they were not detected in the heart. 4. An enzyme that catalyses the oxidation of glycollate was also demonstrated in liver tissue. This had a different electrophoretic mobility from the lactate dehydrogenase isoenzymes. 5. These findings are discussed with particular reference to human primary hyperoxaluria in which excessive oxalate synthesis occurs.

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