FEBS Letters | |
Phospholipase C in rat liver plasma membranes | |
Melin, Per-Martin1  Jergil, Bengt1  Sundler, Roger2  | |
[1] >Biochemistry, Chemical Centre, Box 124, University of Lund, Box 94, S-221 00 Lund, Sweden;Medical and Physiological Chemistry, University of Lund, Box 94, S-221 00 Lund, Sweden | |
关键词: Ca2+; Guanine nucleotide; Inositol trisphosphate; Phosphatidylinositol bisphosphate; Phospholipase C (Rat liver plasma membrane); GMP-PCP; guanylyl (β; γ-methylene)diphosphonate; IP2; myo-inositol bisphosphate; IP3; myo-inositol trisphosphate; PI; phosphatidylinositol; PIP; phosphatidylinositol 4-phosphate; PIP2; phosphatidylinositol 4; 5-bisphosphate; | |
DOI : 10.1016/0014-5793(86)81189-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Phospholipase C activity against phosphoinositides in isolated rat liver plasma membranes has been examined using exogenous substrates. The enzyme hydrolyzed phosphatidylinositol 4,5-bisphosphate 30–40-times faster than phosphatidylinositol 4-monophosphate, while phosphatidylinositol was not a substrate. Maximum activity was observed with 1.1 mM phosphatidylinositol 4,5-bisphosphate at pH 5.0. The enzyme was stimulated by micromolar concentrations of Ca2+. The GTP analogue guanylyl (β,γ-methylene)diphosphonate enhanced phospholipase C activity at and above 0.3 μM Ca2+, but was inhibitory at 0.1 μM Ca2+. This supports the suggestion that plasma membrane phospholipase C is regulated by guanine nucleotide-binding protein, but indicates a regulatory mechanism different from that of other enzymes regulated by such proteins.
【 授权许可】
Unknown
【 预 览 】
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