Skip to main content
Log in

Physicochemical properties of cotton-leaf peroxidase

  • Published:
Chemistry of Natural Compounds Aims and scope

Abstract

The physicochemical properties of peroxidase isolated from cotton leaves were investigated. The optimal pH value for exhibiting activity was 4.7; temperature, 30°C. The Michaelis constant was 2.3 mM. Cotton-leaf peroxidase has a very high affinity for benzidine.

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

  1. I. G. Gazaryan (1992) Progress in Science and Technology. Biotechnology VINITI Moscow 4

    Google Scholar 

  2. V. V. Urmantsev (1992) Progress in Science and Technology. Biotechnology VINITI Moscow 54

    Google Scholar 

  3. V. A. Andreeva (1988) Peroxidase Enzyme Nauka Moscow 128

    Google Scholar 

  4. M. Misawa S. M. Martin (1972) Can. J. Biol. 50 1245

    Google Scholar 

  5. C. H. R. Smith R. van Huystee (1989) J. Plant Physiol. 135 391

    Google Scholar 

  6. A. N. Boyarkin (1951) Biokhimiya 16 IssueID7 352

    Google Scholar 

  7. B. J. Davis (1964) Ann. N. Y. Acad. Sci. 121 IssueID2 404

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Translated from Khimiya Prirodnykh Soedinenii, No. 5, pp. 416–418, September–October, 2004.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Akhunov, A.A., Golubenko, Z., Beresneva, Y.V. et al. Physicochemical properties of cotton-leaf peroxidase. Chem Nat Compd 40, 506–509 (2004). https://doi.org/10.1007/s10600-005-0022-1

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10600-005-0022-1

Key words

Navigation