Anderson G R, Kovacik W P
Proc Natl Acad Sci U S A. 1981 May;78(5):3209-13. doi: 10.1073/pnas.78.5.3209.
An unusual isozyme of lactate dehydrogenase (LDH; L-lactate:NAD+ oxidoreductase, EC 1.1.1.27), LDHk, has been described in cells transformed by the Kirsten murine sarcoma virus (KiMSV). This isozyme appears to contain one or more subunits encoded by the transforming gene of KiMSV and is readily distinguished from other isozymes of LDH. Specifically, it is more basic than other LDH isozymes, has an apparent subunit structure of (35,000)4(22,000)1, is essentially inactive if assayed under a normal atmosphere, and is strongly inhibited by GTP and various related compounds. We have examined human cancer and normal tissue controls for expression of an activity like LDHk. In 11 out of 16 human carcinomas, LDHk activity was increased 10- to 500-fold over the level seen in adjoining nontumor tissue. In contrast, other LDH isozymes were increased by only 2- to 5-fold.
一种不寻常的乳酸脱氢酶（LDH；L-乳酸：NAD⁺氧化还原酶，EC 1.1.1.27）同工酶，即LDHk，已在被 Kirsten 小鼠肉瘤病毒（KiMSV）转化的细胞中被描述。这种同工酶似乎包含由 KiMSV 的转化基因编码的一个或多个亚基，并且很容易与其他 LDH 同工酶区分开来。具体而言，它比其他 LDH 同工酶的碱性更强，具有明显的亚基结构(35,000)4(22,000)1，如果在正常大气条件下进行测定，基本上没有活性，并且受到 GTP 和各种相关化合物的强烈抑制。我们已经检测了人类癌症组织和正常组织对照中类似 LDHk 活性的表达情况。在 16 例人类癌症中，有 11 例的 LDHk 活性比相邻非肿瘤组织中的水平增加了 10 至 500 倍。相比之下，其他 LDH 同工酶仅增加了 2 至 5 倍。
