Ketchum C H, Robinson C A, Hall L M, Grizzle W E, Maclaren N K, Riley W J, Trost C
Clin Chem. 1984 Jan;30(1):46-9.
We report nine patients with a sixth band, migrating cathodic to lactate dehydrogenase 5, appearing on routine electrophoresis for serum lactate dehydrogenase (LD, EC 1.1.1.27). Eight of these patients died during their hospitalization. Acidosis, hypotension, and sepsis were the common clinical conditions preceding the band's appearance. In several cases the band appeared transiently. We examined tissue samples from two of the cases, finding LD-6 in liver and skeletal muscle but not in heart. In randomly selected autopsy tissues, LD-6 was detected consistently in liver and skeletal muscle, sometimes in spleen, kidney, and adrenal tissue, but never in heart. Biochemical studies indicate that the LD-6 isoenzyme is not an artifact or an immunoglobulin complex, is larger than the other LD isoenzymes, contains an M-subunit but not an H-subunit, has an isoelectric point in the pH range of 9.0-9.6, and is more heat stable than LD-5.
我们报告了9例在血清乳酸脱氢酶(LD,EC 1.1.1.27)常规电泳时出现第六条带的患者,该条带向阴极迁移至乳酸脱氢酶5区。其中8例患者在住院期间死亡。酸中毒、低血压和败血症是该条带出现之前常见的临床情况。在几例病例中,该条带短暂出现。我们检查了其中2例的组织样本,在肝脏和骨骼肌中发现了LD-6,但在心脏中未发现。在随机选择的尸检组织中,肝脏和骨骼肌中始终能检测到LD-6,有时在脾脏、肾脏和肾上腺组织中也能检测到,但在心脏中从未检测到。生化研究表明,LD-6同工酶不是假象或免疫球蛋白复合物,比其他LD同工酶更大,含有M亚基但不含H亚基,等电点在pH 9.0 - 9.6范围内,并且比LD-5更耐热。