Skip to main content
Log in

Genetic studies on pancreatic proteinase in Japanese quail

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

A genetic variation was found in pancreatic proteinase of Japanese quail. In eight bands of proteinase isozymes, the variation of band 5 (presence or absence) was detected among quails. Band 5 was identified as a chymotrypsin. The presence and absence of band 5 are controlled by a pair of allelic genes (Prt-5 A andPrt-5 a) on an autosomal locus, and genePrt-5 A, causing expression of band 5, is dominant to genePrt-5 a, a null allele for band 5. Zymograms of proteinases and their zymogens were also compared; no variation of chymotrypsinogen; corresponding to chymotrypsinPrt-5 was detected. It is suggested that thePrt-5 variant of chymotrypsin may be formed during activation of chymotrypsinogen.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Blow, D. W. (1971).The Enzymes, Vol. 3 Academic Press, New York.

    Google Scholar 

  • Hou, D.-X., Maeda, Y., Okamoto, S., and Hashiguchi, T. (1988a). The optimal conditions for activation of trypsinogen and chymotrypsinogen of pancreas in coturnix quail.Mem. Fac. Agr. Kagoshima Univ. 24173.

    Google Scholar 

  • Hou, D.-X., Maeda, Y., Fukunaga, T., Okamoto, S., and Hashiguchi, T. (1988b). The activities of pancreatic trypsin and chymotrypsin in coturnix quail lines selected for body weight.Jpn. J. Zootech. Sci. 59896.

    Google Scholar 

  • Hummel, B. C. W. (1959). A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin.Can. J. Biochem. Physiol. 371393.

    Google Scholar 

  • Miller, G. L. (1959). Protein determination for large numbers of samples.Anal. Chem. 31964.

    Google Scholar 

  • Ogita, Z. (1964). Improved agar gel media for thin layer electrophoresis.Med. J. Osaka Univ. 15143.

    Google Scholar 

  • Rick, W. (1974). Chymotrypsin. In Bergmeyer, H. U. (ed.),Methods of Enzymatic Analysis Verlag Chemie Weinheim, Academic Press, New York.

    Google Scholar 

  • Takahashi, A., Tanaka, H., Tamada, S., Shibata, H., and Inagaki, J. (1974). Genetic variations of pancreatic proteinase in pigs.Bull. Aichi-Ken Agr. Res. Center Ser. E (Anim. Indust.) 427.

    Google Scholar 

  • Watanabe, T., and Tomita, T. (1974). Genetic study of pancreatic proteinase and α-amylase in mice (Mus musculus).Biochem. Genet. 12419.

    Google Scholar 

  • Watanabe, T., Ogasawara, N., and Goto, H. (1976). Genetic study of pancreatic proteinase in mice (Mus musculus): Genetic variants of trypsin and chymotrypsin.Biochem. Genet. 14697.

    Google Scholar 

  • Watanabe, T., Miyashita, N., Moriwaki, K., and Hilgers, J. (1986). Evolutionary relationships between laboratory mice and subspecies ofMus musculus based on the genetic study of pancreatic proteinase loci,Prt-1, Prt-2, Prt-3, andPrt-6.Biochem. Genet. 25239.

    Google Scholar 

  • Wright, H. T., Kraut, J., and Wilcox, P. E. (1968). Comparison of the π-, δ-, and τ-chymotrypsin family with α-chymotrypsin.J. Mol. Biol. 37363.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hou, DX., Maeda, Y., Okamoto, S. et al. Genetic studies on pancreatic proteinase in Japanese quail. Biochem Genet 27, 469–479 (1989). https://doi.org/10.1007/BF00553913

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00553913

Key words

Navigation