Herrmann G, Crotet V, Maly I P, Sasse D
Anatomisches Institut der Universität, Basel, Switzerland.
Histochem J. 1994 Jul;26(7):597-600. doi: 10.1007/BF00158594.
A newly developed technique was used for the electrophoretic separation of lactate dehydrogenase (LDH) isoenzymes from lyophilized tissue samples in the nanogram range. In this study portions of 10-200 ng from the myocardium and the conducting system of cattle, sheep, pig and man were microdissected and analysed. In the heart tissues of cattle, sheep and pig, the isoforms LDH1, LDH2 and LDH3 were detected in species-specific varying amounts. In all these animals, the conducting system is marked by high LDH1 activity, which is present at a ratio of about 2:1 compared with the myocardium. The values in man, however, differ from these values, but this might be due to post-mortem changes. The findings are discussed with respect to possible aerobic-anaerobic functions.
一种新开发的技术被用于从纳克级冻干组织样本中电泳分离乳酸脱氢酶(LDH)同工酶。在本研究中,对牛、羊、猪和人的心肌及传导系统中10 - 200纳克的部分进行了显微切割和分析。在牛、羊和猪的心脏组织中,检测到了不同物种含量各异的LDH1、LDH2和LDH3同工型。在所有这些动物中,传导系统的特点是LDH1活性高,与心肌相比,其比例约为2:1。然而,人类的这些值与上述值不同,但这可能是由于死后变化所致。针对可能的有氧 - 无氧功能对这些发现进行了讨论。