Concentration-dependent dissociation/association of human prostatic acid phosphatase
| Autor: | Ewa Luchter-Wasylewska, Klaus-Heinrich Röhm, Marcin Wasylewski |
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| Rok vydání: | 2003 |
| Předmět: |
Male
Acid Phosphatase air-turbine ultracentrifugation tryptophan fluorescence Biochemistry Dissociation (chemistry) chemistry.chemical_compound Bioorganic chemistry Animals Humans Horses Equilibrium Centrifugation Fluorescent Dyes air-turbine ultra- centrifugation chemistry.chemical_classification Chromatography Molecular mass active subunits Fluorescence Molecular Weight Enzyme Monomer Spectrometry Fluorescence chemistry Prostatic acid phosphatase human prostate acid phosphatase dissociation-association Thermodynamics Cattle Protein Tyrosine Phosphatases |
| Zdroj: | Journal of protein chemistry. 22(3) |
| ISSN: | 0277-8033 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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