Lactate dehydrogenase and its isoenzymes in organs and tissues of cattle
2012
Heinová, D., University of Veterinary Medicine and Pharmacy in Košice | Janíková, K. | Kostecká, Z.
We determined the specific activity of lactate dehydrogenase(LDH) in samples from the heart and skeletal muscles and the liver of cattle by the method of Bradford. The electrophoretic separation of the heart muscle LDH in 8—25 % gradient polyacrylamide gel showed that the predominating anode fractions were; LDH1, LDH2 and LDH3 (23 %, 30 % and 24 %, respectively). Of the cathode fractions, we observed only LDH4 (15 %), while LDH5 was not detected. The individual LDH isoenzymes in the skeletal muscle were quite balanced (between 19 and 21 %). A characteristic feature of LDH isoenzymes in the liver of cattle was that the majority were from the anode fractions, LDH1, LDH2 and LDH3 (27 %, 25 % and 20 %, respectively),while the cathode fractions exhibited a lower catalytic intensity(15 % for LDH4 and 12.5 % for LDH5). This picture of LDH in the liver and skeletal muscles pointed to the need to evaluate these enzymes also in relation to other biological species.
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