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

Research output: Contribution to Journal/MagazineJournal article

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Phosphatidylinositol 4,5-bisphosphate specific phospholipase C in Pharbitis nil membranes. / Bonner, P. L. R.; Prior, S.; Hetherington, A. M. et al.
In: Biologia Plantarum, Vol. 34, No. 5-6, 1992, p. 367-372.

Research output: Contribution to Journal/MagazineJournal article

Harvard

Bonner, PLR, Prior, S, Hetherington, AM & Lumsden, PJ 1992, 'Phosphatidylinositol 4,5-bisphosphate specific phospholipase C in Pharbitis nil membranes.', Biologia Plantarum, vol. 34, no. 5-6, pp. 367-372. https://doi.org/10.1007/BF02923581

APA

Bonner, P. L. R., Prior, S., Hetherington, A. M., & Lumsden, P. J. (1992). Phosphatidylinositol 4,5-bisphosphate specific phospholipase C in Pharbitis nil membranes. Biologia Plantarum, 34(5-6), 367-372. https://doi.org/10.1007/BF02923581

Vancouver

Bonner PLR, Prior S, Hetherington AM, Lumsden PJ. Phosphatidylinositol 4,5-bisphosphate specific phospholipase C in Pharbitis nil membranes. Biologia Plantarum. 1992;34(5-6):367-372. doi: 10.1007/BF02923581

Author

Bonner, P. L. R. ; Prior, S. ; Hetherington, A. M. et al. / Phosphatidylinositol 4,5-bisphosphate specific phospholipase C in Pharbitis nil membranes. In: Biologia Plantarum. 1992 ; Vol. 34, No. 5-6. pp. 367-372.

Bibtex

@article{5c57e3a95de342fc882cbf51a90c29c2,
title = "Phosphatidylinositol 4,5-bisphosphate specific phospholipase C in Pharbitis nil membranes.",
abstract = "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.",
author = "Bonner, {P. L. R.} and S. Prior and Hetherington, {A. M.} and Lumsden, {P. J.}",
year = "1992",
doi = "10.1007/BF02923581",
language = "English",
volume = "34",
pages = "367--372",
journal = "Biologia Plantarum",
issn = "0006-3134",
publisher = "Springer Netherlands",
number = "5-6",

}

RIS

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 -