Saavedra R A, Anderson G R
Science. 1983 Jul 15;221(4607):291-2. doi: 10.1126/science.6857286.
An unusual isozyme of lactate dehydrogenase, lactate dehydrogenase k, is found in high concentrations in cultured cells transformed by the Kirsten murine sarcoma virus and in many human cancer tissues. In experiments described here high levels of a lactate dehydrogenase k activity were detected in extracts of normal rodent retina. This activity had the same key properties as the human tumor isozyme, namely, a highly cathodic electrophoretic mobility and inhibition of enzymatic activity by oxygen and 5',5'-dipurinenucleoside tetraphosphates. Expression of this activity in the retina may be related to the high aerobic glycolysis characteristic of the retina, a metabolic feature shared with many tumors.
一种不寻常的乳酸脱氢酶同工酶——乳酸脱氢酶K，在被 Kirsten 小鼠肉瘤病毒转化的培养细胞以及许多人类癌症组织中含量很高。在本文所述的实验中，在正常啮齿动物视网膜提取物中检测到了高水平的乳酸脱氢酶K活性。这种活性具有与人类肿瘤同工酶相同的关键特性，即高度阴极电泳迁移率以及被氧气和5',5'-二嘌呤核苷四磷酸抑制酶活性。这种活性在视网膜中的表达可能与视网膜特有的高有氧糖酵解有关，这是许多肿瘤共有的代谢特征。
