Otsu N, Hirata M, Miyazawa K, Tuboi S
Clin Chem. 1985 Feb;31(2):318-20.
Serum and tumor tissue of a patient with neuroblastoma contained an abnormal isoenzyme of lactate dehydrogenase (LDH; EC 1.1.1.27), which, on agarose gel electrophoresis, migrated between LDH-2 and LDH-3 with a mobility the same as that of the extra LDH isoenzyme found in normal human erythrocytes. On surgical removal of the tumor, the high total LDH activity (775 U/L) in the serum of the patient rapidly decreased to normal (70-220 U/L), and the abnormal LDH isoenzyme was no longer detected. The total LDH activity of the abnormal LDH isoenzyme per gram of hemoglobin in the tumor tissue was 26 times that of erythrocytes, suggesting that the abnormal isoenzyme originated mainly from the tumor cells themselves rather than the erythrocytes contained in the tumor tissue. This first report on the appearance of the abnormal LDH isoenzyme in a patient with neuroblastoma suggests that this abnormal LDH isoenzyme may have some significance as a marker enzyme for neurogenic tumors.
一名神经母细胞瘤患者的血清和肿瘤组织中含有乳酸脱氢酶(LDH;EC 1.1.1.27)的异常同工酶,在琼脂糖凝胶电泳中,其迁移位置在LDH-2和LDH-3之间,迁移率与正常人红细胞中发现的额外LDH同工酶相同。手术切除肿瘤后,患者血清中较高的总LDH活性(775 U/L)迅速降至正常水平(70 - 220 U/L),且异常LDH同工酶不再被检测到。肿瘤组织中每克血红蛋白的异常LDH同工酶总活性是红细胞的26倍,这表明异常同工酶主要起源于肿瘤细胞本身,而非肿瘤组织中所含的红细胞。这篇关于神经母细胞瘤患者出现异常LDH同工酶的首次报告表明,这种异常LDH同工酶可能作为神经源性肿瘤的标记酶具有一定意义。