Skip to main content
Log in

A simultaneous-coupling azo dye method for the quantitative assay of esterase using α-naphthyl acetate as substrate

  • Papers
  • Published:
The Histochemical Journal Aims and scope Submit manuscript

Summary

This paper describes a simultaneous-couplng azo dye method for the measurement of estarase activity using the histochemical substrate, α-naphthyl acetate. By the choice of two diazonism salts with optimal coupling characteristics, the reaction be carried out at any pH between 3.0 and 9.5. The azo dye is maintained in solution for spectrophotometric measurements with bovine serum albumin. The simultaneous-coupling method is compared with an assay based on the direct measurement of released α-naphthol by its ultra-violet bsorbance in a pH study of hog liver esterase. There is good agreement between the data obrained by both methods.

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

  • Berger, W. C., Prentice, N., Moeller, M. &Kastenschmidt, J. (1970) Hydrolysis of alpha naphthyl acetate andl-leucyl naphthylamide by barley enzymes.Phytochemistry 9, 33–40.

    Google Scholar 

  • Burlina, A. &Galzigna, L. (1972) A new and simple procedure for serum arylesterase.Clinica chim. Acta 39, 255–7.

    Google Scholar 

  • Burstone, M. S. (1962)Enzyme Histochemistry and its Application to the Study of Neoplasms. New York: Academic Press.

    Google Scholar 

  • Comori, G. (1953) Human esterases.J. Lab. clin. Med. 42, 445–53.

    Google Scholar 

  • Hopsu, M. D. &Glenner, G. G. (1963) A histochemical enzyme kinetic system applied to the trypsin-like amidase and esterase activity in human mast cells.J. Cell Biol. 17, 503–20.

    Google Scholar 

  • Hopsu, M. D. &McMillan, P. J. (1964) Quantitative characterization of a histochemical enzyme system.J. Histochem. Cytochem. 12, 315–24.

    Google Scholar 

  • Huggins, C. &Lapides, J. (1974) Chromogenic substrates. IV. Acylesters ofp-nitrophenol as substrates for colorimetric determination of esterase.J. biol. Chem. 170, 467–82.

    Google Scholar 

  • James, D. J. &Smith, A. R. W. (1974) A biochemical study of non-specific esterases from plant cells, employing the histochemical substrate, naphthol AS-D acetate.Histochem. J. 6, 7–23.

    Google Scholar 

  • Jarrett, A. &Please, N. W. (1970) A quantitative histochemical technique for the estimation of azo dye coupling reactions.Histochem. J. 2, 297–313.

    Google Scholar 

  • Pearse, A. G. E. (1968)Histochemistry: Theoretical and Applied. Vol. 1. 3rd edn. Edinburgh, London: Churchill Livingstone.

    Google Scholar 

  • Robinson, B. (1977) SPSS, subprogram non-linear regression. NUCC Manual No. 433. Supplement toStatistical Package for the Social Sciences. 2nd edn. (edited byNie, N. H., Hull, C. H., Jenkins, J. G., Steinbrenner, K. andBent, D. H.), New York: McGraw Hill (1975).

    Google Scholar 

  • Rutenburg, A. M. &Seligman, A. M. (1956) Protein binding of azo dyes by tissue homogenates.J. Histochem. Cytochem. 4, 17–22.

    Google Scholar 

  • Seligman, A. M. &Nachlas, M. M. (1950) The colorimetric determination of lipase and esterase in human serum.J. clin Invest. 29, 31–6.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Johnston, K.J., Ashford, A.E. A simultaneous-coupling azo dye method for the quantitative assay of esterase using α-naphthyl acetate as substrate. Histochem J 12, 221–234 (1980). https://doi.org/10.1007/BF01024552

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01024552

Keywords

Navigation