Heinová Dagmar, Kostecká Zuzana, Csank Tomáš
Department of Chemistry, Biochemistry and Biophysics, University of Veterinary Medicine and Pharmacy, Košice, Slovakia.
Department of Microbiology and Immunology, University of Veterinary Medicine and Pharmacy, Košice, Slovakia.
Electrophoresis. 2016 Jan;37(2):335-8. doi: 10.1002/elps.201500407. Epub 2015 Dec 15.
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.
在pH 8.8条件下进行的天然聚丙烯酰胺凝胶电泳无法分离火鸡来源的乳酸脱氢酶(LDH)同工酶。使用等电聚焦(IEF)技术,在pH 3 - 9范围内,在火鸡的血清和组织中检测到了该酶的五种电泳可区分形式。一般来说,可观察到三个不同的组:(i)那些具有阳极优势的(心脏、肾脏、胰腺和红细胞),主要是LDH - 1组分;(ii)那些具有阴极优势的(胸肌和血清),以LDH - 5为主;(iii)那些分布较为均匀的(肝脏、脾脏、肺和大脑)。酶的比活性在胸肌中最高,其次是心肌和大脑。在血清、肾脏和肝脏中检测到的活性较低。