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The Ames Test for Carcinogens
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However, the strain will grow if a mutagen is added to the medium, causing the defective gene in the histidine pathway to revert to the wild-type. (Mutagens inducing gross chromosomal damage, such as deletions or inversions, will not be detected.) Under normal circumstances, there is a background mutation rate; a certain number of Salmonella cells revert spontaneously, and therefore a certain number of colonies will grow on the minimal medium. A mutagen, however, increases the number of colonies that can grow on minimal medium.This procedure is, therefore, a rapid, inexpensive, and easy test for mutagenicity. To improve this test s ability to detect carcinogens, Ames added a supplement of rat liver extract to the medium. It is known that, although many substances are themselves not carcinogens, the breakdown of these substances in the liver creates substances that are carcinogenic. Rat liver enzymes act on a substance the same way human livers do, converting a noncarcinogenic primary substance into a possible carcinogen. The liver enzymes can also make a mutagen nonmutagenic.
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Other short-term tests are in use that effectively duplicate the Ames test. These include tests for mutagenicity in mouse lymphoma cells and two tests in Chinese hamster ovary cells: a test for chromosomal aberrations and a test for sisterchromatid exchanges. None of these tests surpasses the Ames test, which has scored better than 90% correct when tested with hundreds of known carcinogens. Thousands of other substances have been subjected to this test; many have proven to be mutagenic. These substances are usually withdrawn from the workplace or home environment. From time to time, we read that a certain substance is believed to be carcinogenic and is being removed from grocery store shelves. Examples have included hair dyes, food preservatives, food-coloring agents, and arti cial sweeteners. Many of these rst were suspected after they failed the Ames test.
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Bruce Ames (1928 ).
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(Courtesy Dr. Bruce Ames.)
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III. Molecular Genetics
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12. DNA: Its Mutation, Repair, and Recombination
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Mutation
BOX 12.2
ne way of studying the way that proteins work is to change the sequence of amino acids in the protein. For example, if a scientist were working on the active site of a particular enzyme, he or she could learn how the enzyme modifies its substrates by changing one or a few amino acids. Changes could be made, for example, in order to study the role of shape or charge on the functioning of the enzyme. Advances in recombinant DNA techniques have made it possible for a research scientist to create exactly the changes he or she wants in a protein. To begin with, the gene for the protein or enzyme must be cloned so that it can be manipulated (see chapter 13). Once cloned, deletions are easy to create with restriction en-
Experimental Methods
In Vitro Site-Directed Mutagenesis
donucleases (described in chapter 13). If a particular endonuclease cuts the gene in two places, the intervening segment can be spliced out ( g. 1a; see chapter 13). If the endonuclease cuts only once, exonucleases can digest the ends of the cut, extending the deletion away from the cut in both directions ( g. 1b). Insertions can be created by either cutting the gene and repairing the singlestranded ends ( g. 1c) or by creating
an oligonucleotide (a linker) with the desired sequence and inserting the linker at the site of an endonuclease cut ( g. 1d). Far more impressive, however, is the ability to change a single speci c codon in order to replace any amino acid in the protein with any other amino acid. The process involves directed mutagenesis using arti cially created oligonucleotides. Basically, a short sequence of DNA (an oligonucleotide) is synthesized complementary to a region of the cloned gene, but with a change in one or more bases of a codon to specify a different amino acid. That oligonucleotide is then hybridized with the single-stranded form of the clone ( g. 2). Although one or more
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