Faculty of Pharmaceutical Sciences, Toho University, 2-2-1 Miyama, Funabashi, 274-8510, Japan.
Mar Biotechnol (NY). 2011 Apr;13(2):137-41. doi: 10.1007/s10126-010-9299-6. Epub 2010 Jun 1.
The effects of high hydrostatic pressure on lactate dehydrogenase (LDH) activities from two species of hagfish were examined. LDH from Eptatretus okinoseanus, a deep-sea species, retained 67% of the original activity even at 100 MPa. LDH activity from Eptatretus burgeri, a shallow-sea species, was completely lost at 50 MPa but recovered to the original value at 0.1 MPa. The tetrameric structure of LDH-A(4) from E. okinoseanus did not change at 50 MPa. In contrast, almost all LDH tetramers from E. burgeri dissociated to dimers and monomers at 50 MPa but reverted to tetramers at 0.1 MPa. These results show that the dissociation of tetramers caused the inactivation of E. burgeri LDH. The difference depends on the number 6 and 10 amino acids. The mechanism of the slight, gradual inactivation of E. okinoseanus LDH at high pressure differs and is probably due to the metamorphosis of its inner structures.
本研究考察了两种盲鳗的乳酸脱氢酶（LDH）在高压下的变化。来自深海物种欧氏盲鳗（Eptatretus okinoseanus）的 LDH 在 100 MPa 下仍保持 67%的原始活性。来自浅海物种伯氏盲鳗（Eptatretus burgeri）的 LDH 在 50 MPa 下完全失活，但在 0.1 MPa 下恢复到原始水平。在 50 MPa 下，来自欧氏盲鳗的 LDH-A(4)的四聚体结构没有改变。相比之下，伯氏盲鳗的几乎所有 LDH 四聚体在 50 MPa 下解离为二聚体和单体，但在 0.1 MPa 下又重新形成四聚体。这些结果表明，四聚体的解离导致伯氏盲鳗 LDH 的失活。这种差异取决于 6 号和 10 号氨基酸。深海物种欧氏盲鳗 LDH 在高压下缓慢逐渐失活的机制不同，可能与其内部结构的变化有关。
