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Phosphatidylinositol 4,5-bisphosphate specific phospholipase C in Pharbitis nil membranes.

Research output: Contribution to Journal/MagazineJournal article

  • P. L. R. Bonner
  • S. Prior
  • A. M. Hetherington
  • P. J. Lumsden
<mark>Journal publication date</mark>1992
<mark>Journal</mark>Biologia Plantarum
Issue number5-6
Number of pages6
Pages (from-to)367-372
Publication StatusPublished
<mark>Original language</mark>English


Phosphatidylinositol 4,5-bisphosphate specific phospholipase C has been detected in a membrane preparation fromPharbitis nil cotyledons. The enzyme has a pH optimum of 6.8 and activated by calcium ions, deoxycholate, phosphatidylinositol and phosphatidylethanolamine. The enzyme is inhibited to varying degrees by Tween 20, Triton XI00, zinc, copper, cobalt and manganese ions and phosphatidylserine. G-protein activators do not affect the activity ofPharbitis nil phospholipase C. Analysis of the products of the reaction by HPLC shows inositol 1,4,5-trisphosphate from phospholipase C and inositol bisphosphate from inositol-1 and -5 phosphatase activity.