Research output: Contribution to Journal/Magazine › Journal article
Research output: Contribution to Journal/Magazine › Journal article
}
TY - JOUR
T1 - Phosphatidylinositol 4,5-bisphosphate specific phospholipase C in Pharbitis nil membranes.
AU - Bonner, P. L. R.
AU - Prior, S.
AU - Hetherington, A. M.
AU - Lumsden, P. J.
PY - 1992
Y1 - 1992
N2 - 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.
AB - 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.
U2 - 10.1007/BF02923581
DO - 10.1007/BF02923581
M3 - Journal article
VL - 34
SP - 367
EP - 372
JO - Biologia Plantarum
JF - Biologia Plantarum
SN - 0006-3134
IS - 5-6
ER -