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

Cooper, Rosemary A., Bowen, I. D. and Lloyd, D. ORCID: https://orcid.org/0000-0002-5656-0571 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:	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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