Release and activation of a particulate bound acid phosphatase from Tetrahymena pyriformis.
A sedimentable form of acid phosphatase (EC 3.1.3.2) from Tetrahymena pyriformis was found to be solubilized by Triton X-100. The total enzyme activity in the insoluble cell fraction increased almost 200% upon solubilization with Triton X-100 or Nonidet P-40. Removal of membrane lipids and Triton X-100 from the particulate wash solution with a chloroform extraction resulted in non-specific enzyme-protein aggregation which was reversible upon addition of Triton X-100. The results indicate that this acid phosphatase is an integral membrane protein. The pH optima for this particulate bound acid phosphatase was 3.5 with o-carboxyphenyl phosphate and 4.0 with p-nitrophenyl phosphate as substrates. The Km values of each substrate were 3.1 and 0.031 mM, respectively.
D000135:Acid Phosphatase / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D004789:Enzyme Activation; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D011092:Polyethylene Glycols; D011485:Protein Binding; D012995:Solubility; D013769:Tetrahymena pyriformis / Q000201:enzymology*
D011092:Polyethylene Glycols; D000135:Acid Phosphatase