Evans M J, Plummer M J, Anderson G R
Cancer Res. 1984 Jan;44(1):319-23.
An unusual isozyme of lactate dehydrogenase, originally detected in Kirsten sarcoma virus-infected cells and later shown to be induced in normal mammalian cells by anaerobic shock, has also been reported at elevated levels in several human carcinomas. This enzyme is subject to inhibition by guanosine triphosphate and by the dinucleosides 5',5"'-diadenosine tetraphosphate and 5',5"'-diguanosine tetraphosphate (4). Fluctuation of the activity of this enzyme in soluble extracts of synchronized HeLa cells suggests the enzyme may be linked to DNA synthesis. The lactate dehydrogenase K activity increased in early S phase and then decreased to nearly undetectable levels during the period of most active DNA synthesis. This was observed in cells synchronized by thymidine excess or by aphidicolin, an inhibitor of DNA polymerase alpha.
一种不寻常的乳酸脱氢酶同工酶最初在感染 Kirsten 肉瘤病毒的细胞中被检测到，后来发现正常哺乳动物细胞在厌氧休克时会诱导产生这种同工酶，据报道，在几种人类癌症中其水平也会升高。这种酶会受到三磷酸鸟苷以及二核苷 5',5'''-二磷酸腺苷四磷酸和 5',5'''-二磷酸鸟苷四磷酸的抑制(4)。同步化的 HeLa 细胞可溶性提取物中这种酶活性的波动表明该酶可能与 DNA 合成有关。乳酸脱氢酶 K 的活性在 S 期早期增加，然后在 DNA 合成最活跃的时期降至几乎检测不到的水平。在通过过量胸苷或 DNA 聚合酶α抑制剂阿非迪霉素同步化的细胞中观察到了这种情况。
