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Type I phosphodiesterase in the isolated, brush-border membrane of Hymenolepis diminuta



Type I phosphodiesterase in the isolated, brush-border membrane of Hymenolepis diminuta



Journal of Parasitology 67(5): 617-622



The isolated, brush-border membrane of H. diminuta contained an enzyme which hydrolyzed phosphodiester bonds. This enzyme appeared to be a Type I phosphodiesterase PDase (EC 3.1.4.1) (produces nucleoside 5'-phosphates) and had no activity against synthetic Type II PDase substrates (mononucleotides substituted at the 3' position). The effects of various potential inhibitors of enzymatic activity and cation requirements of this enzyme demonstrated a distinct difference between the PDase and alkaline phosphatase activities of the isolated, brush-border membrane. SDS sodium dodecyl sulfate -polyacrylamide gel electrophoresis of the isolated membrane preparation, followed by localization of PDase activity in the gels, indicated the enzyme had a MW of .apprx. 87,000. The PDase activity represents a previously undescribed, membrane-bound enzyme of the brush-border of H. diminuta.

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Accession: 001026512

Download citation: RISBibTeXText

PMID: 6271942

DOI: 10.2307/3280434


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