The properties and subcellular localization of acid phosphatases in the colourless alga, Polytomella caeca

Cooper, Rosemary A., Bowen, I. D. and Lloyd, D.

1973. The properties and subcellular localization of acid phosphatases in the colourless alga, Polytomella caeca. Journal of Cell Science 15 (3) , pp. 605-618.

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Abstract

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. β-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.

Item Type:	Article
Date Type:	Submission
Status:	Published
Schools:	Schools > Biosciences
Publisher:	Company of Biologists
ISSN:	0021-9533
Last Modified:	26 Oct 2022 08:33
URI:	https://orca.cardiff.ac.uk/id/eprint/127768

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