Skip to main content
Log in

Concentration-Dependent Dissociation/Association of Human Prostatic Acid Phosphatase

  • Published:
Journal of Protein Chemistry Aims and scope Submit manuscript

Abstract

The apparent molecular mass of human prostatic acid phosphatase (PAP) was estimated over a wide range of enzyme concentrations using equilibrium centrifugation in the “Airfuge” tabletop ultra-centrifuge. We show that the average mass of all active PAP species steeply increases at enzyme concentrations around 100 nM. The data indicate that at lower concentrations, active monomer prevail, whereas at concentrations above 100 nM, PAP active dimers are formed. These findings were confirmed by measurements of fluorescence emission intensity as a function of enzyme concentration. A shift of the normalized PAP fluorescence intensity around 100 nM independently indicates that a major structural change of the PAP protein occurs in that range of concentrations. From these findings, we conclude that in dilute solutions, several active PAP species exist, which are involved in concentration-dependent dissociation/association equilibria.

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

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Ewa Luchter-Wasylewska.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Luchter-Wasylewska, E., Wasylewski, M. & Röhm, KH. Concentration-Dependent Dissociation/Association of Human Prostatic Acid Phosphatase. J Protein Chem 22, 243–247 (2003). https://doi.org/10.1023/A:1025016402860

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1025016402860

Navigation