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Journal of Cell Science, Vol 15, 605-618, Copyright © 1974 by Company of Biologists

Submitted on December 4, 1973

The Properties and Subcellular Localization of Acid Phosphatases in the Colourless Alga, Polytomella Caeca

ROSEMARY A. COOPER 1, I. D. BOWEN 2, and D. LLOYD 3

1 Departments of Microbiology and Zoology, University College, Newport Road, Cardiff, CF1 3NR, Wales; Department of Biological and Chemical Sciences, Llandaff College of Technology, Western Avenue, Cardiff, CF5 2YB, Wales
2 Departments of Microbiology and Zoology, University College, Newport Road, Cardiff, CF1 3NR, Wales; Department of Zoology, University College, Cathays Park, Cardiff, CF1 1XL, Wales
3 Departments of Microbiology and Zoology, University College, Newport Road, Cardiff, CF1 3NR, Wales

The acid p-nitrophenyl phosphatase of homogenates of Polytomella caeca is a latent acid hydrolase, which is partially inhibited by NaF. Its distribution profile in density gradients (which is similar to that of naphthyl AS-TR phosphatase) suggests that this enzyme is partially lysosomal in location. Cytochemical evidence for the localization of acid phosphatases in fine subcellular structures is presented. Naphthyl AS-TR phosphatase is localized in vacuoles, points of focal degradation, Golgi bodies and dispersed throughout the cytosol. {beta}-Glycerophosphatase is confined to large vacuoles and the cytosol. The nature of acid phosphatase-containing organelles in P. caeca is discussed in view of the inability to detect eleven other latent acid hydrolases in cell-free homogenates.

Submitted on December 4, 1973






© The Company of Biologists Ltd 1974