金属诱导血红素加氧酶而细胞色素P-450无同时降解。化合物SKF 525A对血红素蛋白的保护作用。
Metal induction of haem oxygenase without concurrent degradation of cytochrome P-450. Protective effects of compound SKF 525A on the haem protein.
作者信息
Drummond G S, Rosenberg D W, Kappas A
出版信息
Biochem J. 1982 Jan 15;202(1):59-66. doi: 10.1042/bj2020059.
Abstract
The induction of hepatic haem oxygenase (EC 1.14.99.3) by a series of metals, organometals and metalloporphyrins was examined in vivo in the presence of compound SKF 525A, which is known to complex with the prosthetic group of cytochrome P-450. Concurrent administration of SKF 525A and an inducing metal did not affect the extent and time course of haem oxygenase induction. The decrease in cytochrome P-450 content normally associated with metal administration was, however, prevented, indicating that haem oxygenase induction by metals can proceed without the significant labilization of the haem moiety of cytochrome P-450. In addition, the integrity of this haem protein can be maintained by chemical means in the presence of sustained high activities of haem oxygenase.
摘要
在已知与细胞色素P - 450辅基结合的化合物SKF 525A存在的情况下，于体内检测了一系列金属、有机金属和金属卟啉对肝血红素加氧酶（EC 1.14.99.3）的诱导作用。同时给予SKF 525A和诱导性金属并不影响血红素加氧酶诱导的程度和时间进程。然而，通常与金属给药相关的细胞色素P - 450含量的降低被阻止了，这表明金属对血红素加氧酶的诱导可以在细胞色素P - 450血红素部分没有明显不稳定的情况下进行。此外，在血红素加氧酶持续高活性存在的情况下，可以通过化学方法维持这种血红素蛋白的完整性。
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