Hostname: page-component-78c5997874-lj6df Total loading time: 0 Render date: 2024-11-10T02:28:32.688Z Has data issue: false hasContentIssue false
  • English
  • Français

Protein and amino acid composition of hair from mice carrying the naked (N) gene

Published online by Cambridge University Press:  14 April 2009

Kathryn A. Raphael ,
R. C. Marshall  and
Pamela R. Pennycuik
Kathryn A. Raphael
Affiliation:
CSIRO, Division of Animal Production, P.O. Box 239, Blacktown, N.S.W., 2148, Australia.
R. C. Marshall
Affiliation:
CSIRO, Division of Protein Chemistry, 343 Royal Parade, Parkville, Victoria, 3052, Australia.
Pamela R. Pennycuik
Affiliation:
CSIRO, Division of Animal Production, P.O. Box 239, Blacktown, N.S.W., 2148, Australia.
Rights & Permissions [Opens in a new window]

Summary

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

The protein and amino acid compositions of hair from mice carrying the naked (N) gene were compared with those of wild-type (+ / +) mouse hair using two-dimensional polyacrylamide gel electrophoresis and amino acid analysis. In samples obtained from N /+ mice, the numbers of positions of the low-sulphur (LS), high-sulphur (HS) and high tyrosine (HT) protein spots were indistinguishable from those observed in + / + samples but the amount of HT protein was reduced in N / + hair. In samples obtained from N /N mice the protein spots were fewer than, and perhaps different from, those in samples from the other two genotypes; all protein classes were represented but the HS and HT protein content appeared to be less than that in + / + and N / + hair. Amino acid analyses of hair samples showed that the HS contents of + / + and N / + hair were approximately the same, whereas the HT protein content of N / + hair was about half that in + / + hair. N / N hair contained less half-cystine and tyrosine than + / + and N / + hairs, but because the contents of proline, threonine and glycine were unexpectedly high, it appears that protein components of unusual composition are present in N / N hair. It was concluded that the gene at the N locus is involved only indirectly in the synthesis of the structural proteins found in mouse hair.

Type
Research Article
Information
Genetics Research , Volume 44 , Issue 1 , August 1984 , pp. 29 - 38
Copyright
Copyright © Cambridge University Press 1984

References

REFERENCES

Bendit, E. G. & Gillespie, J. M. (1978). The probable role and location of high-glycine-tyrosine proteins in the structure of keratins. Biopolymers 17, 2743–2745.CrossRefGoogle ScholarPubMed
Bonner, W. M. & Laskey, R. A. (1974). A film detection method for tritium-labelled proteins and nucleic acids in polyacrylamide gels. European Journal of Biochemistry 46, 83–88.CrossRefGoogle ScholarPubMed
Fraser, R. D. B., Gillespie, J. M. & Macrae, T. P. (1973). Tyrosine-rich proteins in keratins. Comparative Biochemistry and Physiology 44B, 943–947.Google ScholarPubMed
Fraser, R. D. B., Macrae, T. P. & Rogers, G. E. (1972). Keratins, Their Composition, Structure and Biosynthesis. Springfield, Illinois: Charles C. Thomas.Google Scholar
Frenkel, M. J., Gillespie, J. M. & Reis, P. J. (1974). Factors influencing the biosynthesis of the tyrosine-rich proteins of wool. Australian Journal of Biological Sciences 27, 31–38.CrossRefGoogle ScholarPubMed
Frenkel, M. J., Gillespie, J. M. & Reis, P. J. (1975). Studies on the inhibition of synthesis of the tyrosine-rich proteins of wool. Australian Journal of Biological Sciences 28, 331–338.CrossRefGoogle ScholarPubMed
Gillespie, J. M. (1972). Proteins rich in glycine and tyrosine from keratins. Comparative Biochemistry and Physiology 41B, 723–734.Google Scholar
Gillespie, J. M. (1983). The structural proteins of hair: isolation, characterization, and regulation of biosynthesis. In Biochemistry and Physiology of the Skin (ed. Goldsmith, L. A.). New York: Oxford University Press.Google Scholar
Gillespie, J. M. & Frenkel, M. J. (1974). The diversity of keratins. Comparative Biochemistry and Physiology 47B, 339–346.Google Scholar
Gillespie, J. M., Frenkel, M. J. & Reis, P. J. (1980). Changes in the matrix proteins of wool and mouse hair following the administration of depilatory compounds. Australian Journal of Biological Sciences 32, 125–136.CrossRefGoogle Scholar
Marshall, R. C. (1981). Analysis of the proteins from single wool fibers by two-dimensional polyacrylamide gel electrophoresis. Textile Research Journal 51, 106–108.CrossRefGoogle Scholar
Marshall, R. C., Frenkel, M. J. & Gillespie, J. M. (1977). High-sulphur proteins in mammalian keratins: a possible aid in classification. Australian Journal of Zoology 25, 121–132.CrossRefGoogle Scholar
Marshall, R. C. & Gillespie, J. M. (1976). High-sulphur proteins from α-keratins. I. Heterogeneity of the proteins from mouse hair. Australian Journal of Biological Sciences 29, 1–10.CrossRefGoogle ScholarPubMed
Marshall, R. C. & Gillespie, J. M. (1982). Comparison of samples of human hair by two-dimensional electrophoresis. Journal of the Forensic Science Society 22, 377–385.CrossRefGoogle Scholar
Raphael, K. A., Chapman, R. E., Frith, P. A. & Pennycuik, P. R. (1982). The structure of hair and follicles of mice carrying the naked (N) gene. Genetical Research 39, 139–148.CrossRefGoogle ScholarPubMed
Tenenhouse, H. S. & Gold, R. J. M. (1976). Loss of a homologous group of proteins in a dominantly inherited ectodermal malformation. Biochemical Journal 159, 149–160.CrossRefGoogle Scholar
Tenenhouse, H. S., Gold, R. J. M., Kachra, Z. & Fraser, F. C. (1974). Biochemical marker in dominantly inherited ectodermal malformation. Nature (London) 251, 431–432.CrossRefGoogle ScholarPubMed