Membrane-associated phospholipase C of Drosophila retina

Hiroko Inoue, Tohru Yoshioka, Yoshiki Hotta

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    Abstract

    Phospholipase C activities against phosphatidylinositol 4,5-bisphosphate and phos-phatidylinositol have been examined using head homogenate of Drosophila visual mutants. In many mutants the enzyme -activities were found to be reduced. The activities against both phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol were always affected in parallel among the mutants, while the activities of other enzymes related to phosphatidylinositol metabolism, such as diacylglycerol kinase, were not. The enzyme was concluded to be membrane-associated and was activated maximally at low Ca2+ concentration (10-7 M), when phosphatidylinositol 4,5-bisphosphate was used as a substrate, while the activity obtained with phosphatidylinositol increased with the Ca2+ concentration up to 10-4 M. The effects of pH on these two enzyme activities differed to some extent.

    Original languageEnglish
    Pages (from-to)91-94
    Number of pages4
    JournalJournal of Biochemistry
    Volume103
    Issue number1
    Publication statusPublished - 1988 Jan

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    ASJC Scopus subject areas

    • Statistics, Probability and Uncertainty
    • Applied Mathematics
    • Physiology (medical)
    • Radiology Nuclear Medicine and imaging
    • Molecular Biology
    • Biochemistry

    Cite this

    Inoue, H., Yoshioka, T., & Hotta, Y. (1988). Membrane-associated phospholipase C of Drosophila retina. Journal of Biochemistry, 103(1), 91-94.