Related Experiment Video
Updated: Jul 24, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
Published on: August 13, 2017
Is the subunit of prostatic phosphatase active? Reversible denaturation of prostatic acid phosphatase
R Kuciel1, A Bakalova, A Mazurkiewicz
1Institute of Medical Biochemistry, N. Copernicus Academy of Medicine, Kraków, Poland.
Abstract:
Prostatic acid phosphatase [E.C. 3.1.3.2.] is a dimeric protein consisting of two identical subunits. This enzyme was denatured in 6 M urea solution at pH 2.5, and kinetical analysis of reactivation by dilution was performed. At low protein concentrations a second-order kinetics for reactivation of phosphatase, with rate constant 8.3 m M-1sec-1, was observed. At higher protein concentrations the reactivation obeyed first-order kinetics. These results seem to exclude the possibility that subunits of the prostatic phosphatase are catalytically active and suggest that the association of two monomers is necessary for full activity.
Related Concept Videos
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Protein Kinases and Phosphatases
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
GTPases and their Regulation
Large G-proteins, also known...
ATP Driven Pumps III: V-type Pumps
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
Activation and Inactivation of G Proteins
The Proteasome Structure
The proteasome is an...

