Lactate dehydrogenase isoenzymes during seasonal adaptations of carnivore fur animals

2000 ◽  
Vol 36 (1) ◽  
pp. 28-36
Author(s):  
L. K. Kozhevnikova ◽  
N. N. Tyutyunnik ◽  
A. R. Unzhakov ◽  
Kh. I. Meldo
Keyword(s):  
Lactate Dehydrogenase ◽  
Seasonal Adaptations ◽  
Fur Animals ◽  
Lactate Dehydrogenase Isoenzymes

scholarly journals LACTATE DEHYDROGENASE ISOENZYMES AND THE REPRODUCTIVE CYCLE IN THE RAT

Reproduction ◽  
1972 ◽  
Vol 30 (3) ◽  
pp. 425-431 ◽  
Author(s):  
C. PATTERSON ◽  
C. J. MASTERS
Keyword(s):  
Lactate Dehydrogenase ◽  
Reproductive Cycle ◽  
Lactate Dehydrogenase Isoenzymes

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.

Lactate Dehydrogenase Isoenzymes in Hyperplasia and Carcinoma of the Prostate: A Clinical Study

1967 ◽  
Vol 98 (6) ◽  
pp. 686-692 ◽  
Author(s):  
M.M. Elhilali ◽  
J.A. Oliver ◽  
A.L. Sherwin ◽  
K.J. Mackinnon
Keyword(s):  
Clinical Study ◽  
Lactate Dehydrogenase ◽  
Carcinoma Of The Prostate ◽  
Lactate Dehydrogenase Isoenzymes

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.

Sign in / Sign up

Export Citation Format

Share Document