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Richard E. Kouri Raymond Kiefer Eugene M. Zimmerman 《In vitro cellular & developmental biology. Plant》1974,10(1-2):18-25
Summary Two methods for determining the hydrocarbon-metabolizing enzyme activity of cultured mammalian cells were compared. The method
designed to measure benzo[a]an-thracene-induced aryl hydrocarbon hydroxylase activity could detect and quantify enzyme activities
in low passage rodent cells, but could not reproducibly detect levels in intermediate or high passage mouse, rat, or human
cells. The method designed to measure the ability of a cell to convert benzo[a]pyrene from an organic-soluble to an aqueous
acetone-soluble form proved to be more reproducible. This technique, when modified, was demonstrated to be an effective screening
test for the detection of those lines with higher levels of hydrocarbon-metabolizing enzymes.
Supported by the Council for Tobacco Research and Contract NIH 70-2068 within the Virus Cancer Program, National Cancer Institute,
National Institutes of Health. 相似文献
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Ribosomes, the universal cellular machines, possess spectacular architecture accompanied by inherent mobility, allowing for their smooth performance as polymerases that translate the genetic code into proteins. The site for peptide bond formation is located within a universal internal semi-symmetrical region, which was identified within all contemporary ribosomes. The high conservation of this region implies its existence irrespective of environmental conditions and indicates that it may represent an ancient RNA molecular apparatus. Hence, we named it the “proto-ribosome”. This prebiotic pocket-like RNA entity is suggested to be capable to accommodate substrates whose stereochemistry enables the creation of chemical bonds. It could have evolved from an earlier catalytic RNA entity that we named the “pre-proto-ribosome”, presumed to be a molecular machine capable of performing various essential tasks in the RNA world, which was snatched by the amino acid invaders for producing proteins. 相似文献
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