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ANALYSIS OF A MOUSE 
-GLOBIN GENE MUTATION INDUCED BY ETHYLNITROSOUREA
R. A. Popp 1, E. G. Bailiff 1, L. C. Skow 2, F. M. Johnson 2, and Susan E. Lewis 3
1 Biology Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37830
2 Laboratory of Biochemical Genetics, National Institute of Environmental Health Sciences, Research Triangle Park, North Carolina 27709
3 Chemistry and Life Sciences Group, Research Triangle Institute, Research Triangle Park, North Carolina 27709
A DBA/2 mouse treated with ethylnitrosourea sired an offspring whose hemoglobin showed an extra band following starch gel electrophoresis. The variant hemoglobin migrated to a more cathodal position in starch gel. Isoelectric focusing indicated that chain 5 of the mutant hemoglobin migrated to a more cathodal position than the normal chain 5 from DBA/2 mice and that the other 
-globin, chain 1, was not affected. On focusing gels the phenotype of the mutant allele, Hbay9, was expressed without dominance to normal chain 5, and Hbay9/Hbay9 homozygotes were fully viable in the laboratory. The molecular basis for the germinal mutation was investigated by analyzing the amino acid sequence of chain 5y9, the mutant form of -chain 5. A single amino acid substitution (His 
Leu) at position 89 was found in chain 5y9. We propose that ethylnitrosourea induced an A T transversion in the histidine codon at position 89 (CAC CTC). This mutation has apparently not been observed previously in humans, mice or other mammals, and its novel occurrence may be indicative of other unusual mutational events that do not ordinarily occur in the absence of specific mutagen exposure.
Accepted on May 19, 1983
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