General paper
Acid phosphatase in planarians (Dugesia lugubris s.l.). Purification and partial characterization of the major enzyme form

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Abstract

  • 1.

    1. The major acid phosphatase form was isolated and partially characterized from planarian Dugesia lugubris s.l.

  • 2.

    2. The enzyme has mol. wt 74,000 as judged by gel filtration chromatography on a Sephadex G-100 column and it is composed of two apparently identical polypeptide chains of 36,000 mol. wt each determined by SDS gel electrophoresis.

  • 3.

    3. The optimum pH, the effect of some modifier substances and thermal stability indicate that the enzyme is similar to the lysosomal high mol. wt acid phosphatase isolated from vertebrate tissues.

  • 4.

    4. The planarian acid phosphatase hydrolyses a wide variety of phosphate esters including phosphoaminoacids.

  • 5.

    5. Cytochemical data showed that acid phosphatase activity in normal planarian tissues is associated mainly with the lysosomes and Golgi apparatus of various cell types.

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