Zobrazeno 1 - 10
of 31
pro vyhledávání: '"J J Volwerk"'
Publikováno v:
Biochemistry. 31:8978-8983
The substrate stereospecificity of phosphatidylinositol-specific phospholipase C from Bacillus cereus is examined using the resolved optical isomers of synthetic myo-inositol 1-(4-nitrophenyl phosphate), a chromogenic substrate for the phospholipase.
Publikováno v:
Journal of Cellular Physiology. 151:613-622
Confluent monolayers of four contact-inhibited mouse fibroblast lines (Swiss 3T3, Balb/c 3T3, NIH 3T3, and C3H10T1/2) were found to have substantial levels of a cell surface phosphatidylinositol-specific phospholipase C (ecto-PLC). In contrast, confl
Publikováno v:
Chemistry and Physics of Lipids. 60:101-110
A chromogenic water-soluble substrate for phosphatidylinositol-specific phospholipase C was synthesized starting from myo -inositol employing isopropylidene and 4-methoxytetrahydropyranyl protecting groups. In this analogue of phosphatidylinositol, 4
Publikováno v:
Chemistry and Physics of Lipids. 56:159-167
A non-hydrolyzable phosphonate analogue of phosphatidyl inositol, racemic myo-inosityl(1)-5-oxa-16-trifluoroacetamidohexadecyl phosphonate, was synthesized. This phosphonate inhibited the activity of phosphatidyl inositol-specific phospholipase C (Pl
Publikováno v:
Biochemistry. 29:8056-8062
The inositol phosphate products formed during the cleavage of phosphatidylinositol by phosphatidylinositol-specific phospholipase C from Bacillus cereus were analyzed by 31P NMR. 31P NMR spectroscopy can distinguish between the inositol phosphate spe
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1042:410-412
Non-hydrolysable analogues of phosphatidylinositol were synthesized and tested as inhibitors of phosphatidylinositol-specific phospholipase C from Bacillus cereus. In these molecules, the phosphodiester bond of phosphatidylinositol hydrolyzed by the
Publikováno v:
Biochemistry. 33(12)
Binding characteristics of phosphatidylinositol-specific phospholipase C (PI-PLC) from Bacillus cereus binding to the phospholipid-water interface were determined by spectroscopic methods and correlated with PI-PLC's catalytic properties. Binding of
Publikováno v:
Analytical biochemistry. 214(2)
A water-soluble, chemiluminescent substrate for sensitive detection of bacterial phosphatidylinositol-specific phospholipase C (PI-PLC) activity was synthesized. This was achieved by replacing the diacylglycerol moiety found in the natural substrate,
Publikováno v:
Journal of neurochemistry. 60(2)
Phosphatidylinositol(PI)-specific phospholipase C activity was detected on the surface of rat astrocytes, rat C6 glioma cells, and rat embryo (REF52) fibroblasts. The cell surface phospholipase C (ecto-PLC) activity was calcium-dependent, did not res
Publikováno v:
Analytical biochemistry. 198(1)
A fluorescent water-soluble substrate for phosphatidylinositol-specific phospholipase C was synthesized. The diacylglycerol moiety of the natural substrate, phosphatidylinositol, was replaced by the fluorescent moiety, 2-naphthol, resulting in the sy