Biochemical correlates of flying behaviour in bats

1978 ◽  
Vol 26 (1) ◽  
pp. 29 ◽  
Author(s):  
BD Muller ◽  
J Baldwin
Keyword(s):  
Lactate Dehydrogenase ◽  
Functional Properties ◽  
Krebs Cycle ◽  
Pectoral Muscle ◽  
Anaerobic Glycolysis ◽  
Krebs Cycle Enzymes ◽  
Lactate Dehydrogenase Isoenzymes

The activities of glycolytic and Krebs cycle enzymes, and the distribution and functional properties of lactate dehydrogenase isoenzymes, were determined in pectoral muscles from a range of bats that differ in flying behaviour. Correlations were found between flying patterns, and the degree to which the pectoral muscle depended upon anaerobic glycolysis during fight.

Maximal activities of hexokinase, 6-phosphofructokinase, oxoglutarate dehydrogenase, and carnitine palmitoyltransferase in rat and avian muscles

1983 ◽  
Vol 3 (12) ◽  
pp. 1149-1153 ◽  
Author(s):  
Eva Blomstrand ◽  
R. A. John Challiss ◽  
Gregory J. Cooney ◽  
Eric A. Newsholme
Keyword(s):  
Domestic Fowl ◽  
Krebs Cycle ◽  
Pectoral Muscle ◽  
Acid Oxidation ◽  
Type I ◽  
Anaerobic Glycolysis ◽  
Significant Activity ◽  
Rat Muscle ◽  
Atp Formation ◽  
Oxoglutarate Dehydrogenase

The maximum activities of 6-phosphofructokinase and oxoglutarate dehydrogenase in muscle provide quantitative indices of the maximum capacities of anaerobic glycolysis and the Krebs cycle (i.e. the aerobic capacity) respectively. These activities were measured in red, white, and cardiac muscle of birds and the rat. The activities in the white pectoral muscle of the domestic fowl suggest that the Krebs cycle plus electron transfer could provide only about 1% of the rate of ATP production provided by anaerobic glycolysis whereas in pigeon pectoral muscle the predicted maximal rates from the two processes are similar. In contrast to domestic-fowl pectoral muscle, the white rat muscle, epitrochlearis, contains a significant activity of oxoglutarate dehydrogenase, which indicates that the Krebs cycle could provide about 12% of the maximum rate of ATP formation. This may be explained by a higher proportion of type-I and -IIA fibres in the rat muscle compared to the avian muscle. In the aerobic muscles of the rat the maximum activities of carnitine palmitoyl transferase indicate that fatty-acid oxidation could provide a high rate of ATP formation.

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.

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
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