Jan 23, 1976

Release and activation of a particulate bound acid phosphatase from Tetrahymena pyriformis

Biochimica Et Biophysica Acta
J T Williams, P S Juo

Abstract

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.

Mentioned in this Paper

Acid Phosphatase
Cataract
Plasma Protein Binding Capacity
Vigilon
Hydrogen-Ion Concentration
Enzyme Activation
Metazoa
Tetrahymena pyriformis

About this Paper

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