نتایج جستجو برای: phosphatidate

تعداد نتایج: 510  

Journal: :The Journal of biological chemistry 2004
Gil-Soo Han Celeste N Johnston George M Carman

The Saccharomyces cerevisiae DPP1-encoded diacylglycerol pyrophosphate phosphatase is a vacuole membrane-associated enzyme that catalyzes the removal of the beta-phosphate from diacylglycerol pyrophosphate to form phosphatidate, and it then removes the phosphate from phosphatidate to form diacylglycerol. The enzyme has six putative transmembrane domains and a hydrophilic region that contains a ...

Journal: :The Biochemical journal 1989
M Freeman E H Mangiapane

When a particle-free supernatant fraction from rat liver was incubated at 37 degrees C with mitochondria and oleate, some of the enzyme phosphatidate phosphohydrolase (PAP), initially present in the particle-free supernatant, was recovered, after the incubation, bound to mitochondria. This translocation of PAP from cytosol to mitochondria was stimulated by oleate or palmitate in a similar fashi...

Journal: :The Biochemical journal 1969
E H Shephard G Hübscher

1. After conventional fractionation of rat liver homogenates in 0.88m-sucrose the mitochondrial fraction was subjected to short-term water lysis followed by separation of the resulting membrane preparations. 2. Phosphatidate formation was measured in all subcellular fractions and subfractions and was compared with the distribution of succinate dehydrogenase, monoamine oxidase, rotenone-insensit...

Journal: :The Journal of biological chemistry 1992
A Malherbe M A Block J Joyard R Douce

Because the envelope phosphatidate phosphatase plays a pivotal role in chloroplast glycerolipid metabolism, we have analyzed whether diacylglycerol could be a regulatory factor of the enzyme. Using isolated envelope membranes in which the level of diacylglycerol was modified by thermolysin treatment of intact chloroplasts to destroy the galactolipid:galactolipid galactosyltransferase, we have d...

Journal: :The Biochemical journal 1978
H P Glenny D N Brindley

1. Male rats were injected daily for 5 days with 0.15m-NaCl, corticotropin, cortisol or l-thyroxine and the rates of glycerolipid synthesis were measured in the livers after intraportal injection of [(14)C]palmitate and [(3)H]glycerol. 2. Injection of all three hormones decreased the rates of body-weight gain. 3. Cortisol treatment increased the weight of the liver relative to body weight. 4. T...

Journal: :Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 2009

Journal: :iranian biomedical journal 0
بهرام حقیقی bahram haghighi محمد یاری mohamad yari شهراز توری shahraz tori

the mechanism by which bi-and trivalent cations affect human liver phosphatidatephosphohydrolase (pap) activity was investigated. bivalent cations up to 1 mm increased pap activity whereas at higher concentrations the activity of the enzyme decreased. the stimulatory concentration for trivalent cations such as al3+ and cr3+, however, was much lower being 2 m m and 1 m m, respectively. all catio...

Journal: :Trends in biochemical sciences 2006
George M Carman Gil-Soo Han

Phosphatidate phosphatase (PAP) enzymes catalyze the dephosphorylation of phosphatidate, yielding diacylglycerol and inorganic phosphate. In eukaryotic cells, PAP activity has a central role in the synthesis of phospholipids and triacylglycerol through its product diacylglycerol, and it also generates and/or degrades lipid-signaling molecules that are related to phosphatidate. There are two typ...

Journal: :The Biochemical journal 1983
D E MacIntyre W K Pollock

Platelet-activating factor stimulates phosphatidylinositol turnover in human platelets as indicated by [32P]phosphatidate accumulation in platelets pre-labelled with [32P]Pi, and by [3H]phosphatidate accumulation and [3H]phosphatidylinositol loss in platelets pre-labelled with [3H]arachidonate. These effects of platelet-activating factor are direct and are independent of the production and/or r...

Journal: :The Biochemical journal 1984
H Holmsen C A Dangelmaier S Rongved

Human platelets incubated with [32P]Pi and [3H]arachidonate were transferred to a Pi-free Tyrode's solution by gel filtration. The labile phosphoryl groups of ATP and ADP as well as Pi in the metabolic pool of these platelets had equal specific radioactivity which was identical to that of[32P]phosphatidate formed during treatment of the cells with thrombin for 5 min. Therefore, the 32P radioact...

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