Separation of turkey lactate dehydrogenase isoenzymes using isoelectric focusing technique

Electrophoresis. 2016 Jan;37(2):335-8. doi: 10.1002/elps.201500407. Epub 2015 Dec 15.

Abstract

Native polyacrylamide gel electrophoresis at pH 8.8 did not allow to separate lactate dehydrogenase (LDH) isoenzymes of turkey origin. Five electrophoretically distinguishable forms of the enzyme were detected in serum and tissues of turkey using IEF technique in a pH range of 3-9. Generally, three different groups were seen: (i) those having an anodic domination (heart, kidney, pancreas, and erythrocytes) with mainly LDH-1 fraction, (ii) those having a cathodic domination (breast muscle and serum) with prevalence of LDH-5, and (iii) those with a more uniform distribution (liver, spleen, lung, and brain). The specific enzyme activity was the highest in the breast muscle, followed by heart muscle, and brain. Low activities were detected in serum, kidney, and liver.

Keywords: Birds; Isoelectric focusing; Lactate dehydrogenase isoenzymes; Mammals; Turkey.

MeSH terms

  • Animals
  • Brain / enzymology
  • Erythrocytes / enzymology
  • Isoelectric Focusing / methods*
  • Isoenzymes / isolation & purification
  • Kidney / enzymology
  • L-Lactate Dehydrogenase / isolation & purification*
  • Lactate Dehydrogenase 5
  • Liver / enzymology
  • Lung / enzymology
  • Myocardium / enzymology
  • Pancreas / enzymology
  • Spleen / enzymology
  • Turkeys* / metabolism

Substances

  • Isoenzymes
  • L-Lactate Dehydrogenase
  • Lactate Dehydrogenase 5
  • lactate dehydrogenase 1