Physiological and pathophysiological alterations in rat hepatic cytochrome P-450.
Physiological and pathophysiological alterations in rat hepatic cytochrome P-450.
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DOI：
10.3109/03602538909103562
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发表时间：
1989
影响因子：
5.9
通讯作者：
J. Schenkman;K. Thummel;L. Favreau
中科院分区：
文献类型：
--
作者：
J. Schenkman;K. Thummel;L. Favreau
Cytochrome P-450 is a large family of related enzymes comprising a number of sub-families. The different cytochrome P-450 enzymes are present in just about every phylum examined for them. They are found in prokaryotes [1], unicellular eukaryotes [2], plants [3], fowl [4], insects [5], fish [6], invertebrates [7], and mammals [8]. While the prokaryotic enzyme, e.g., P-450CAM, is a soluble hemoprotein, that of higher organisms is membrane- bound. In mammals it is located in the mitochondrial inner membrane as well as in the endoplasmic reticulum membranes. In the mammal, different forms of cytochrome P-450 are involved in such diverse reactions as steroid hormone synthesis, at several steps, and the processing of compounds of exogenous origin as well as of endogenous origin for excretion from the body. The enzymes involved in the elimination of compounds are located in the endoplasmic reticulum of most organs and tissues in the body. The very large number of such forms found suggests roles for these other than just broad, overlapping spectra of chemical detoxication.
