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The study investigated the genetic basis of the retarded hair growth (rhg) mutation in mice and identified it as an allele of the ornithine aminotransferase (Oat) gene. Researchers found a specific G to C transversion in the Oat gene associated with the rhg allele, leading to a glycine to alanine substitution. This mutation was shown to be responsible for the retarded hair growth phenotype through genetic crosses with mice carrying a null mutation in Oat. The study also noted that mice with the rhg mutation exhibited chorioretinal degeneration, similar to that seen in OatΔ/OatΔ mice, suggesting that the rhg mutant could serve as a model for studying gyrate atrophy of the choroid and retina (GACR) in humans.

The study investigated the biochemical differences in hair between mice heterozygous for the Naked (N) trait and normal mice. It found that the mutant hair had significantly lower levels of glycine and tyrosine, with 20% less glycine and 27% less tyrosine compared to normal hair. Further analysis showed that proteins extracted from Nn hair contained 30% less glycine and 40% less tyrosine. These findings indicated that the Nn hair was deficient in a specific protein fraction rich in glycine and tyrosine, which comprised about 25% of the total protein in mouse hair. This mutation served as a biochemical marker for a dominantly inherited trait.