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  • 1
    Electronic Resource
    Electronic Resource
    Ethanolamine Base-Exchange Reaction in Rat Brain Microsomal Subfractions (1986)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 46 (1986), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract: Crude microsomal fractions have been subfractionated by differential ultracentrifugation into subtractions A, B, and C, corresponding to light smooth, heavy smooth, and rough microsomal membranes, respectively. The purity and the vesiculation of the membranes were checked biochemically. Subfraction C showed the highest ethanolamine base-exchange activity, both on phospholipid and protein bases. The other two subfractions had roughly similar activities. The kinetic behavior of the enzyme activity, although anomalous, was similar in the three subfractions. Treatment of the vesicles with Pronase or with mercury-dextran produced inactivation of the ethanolamine base-exchange reaction in the three subfractions. These findings suggest that the active site of base-exchange activity would be localized on the external leaflet of the vesicles. Treatment of the membranes with trinitrobenzenesulfonic acid (TNBS) has shown that the newly synthesized phosphatidylethanolamine (PE) belongs to a pool easily reacting with the probe, independent of the subfraction investigated. On the other hand, the distribution of the bulk membrane PE reacting with TNBS differs in the three subfractions examined. It is concluded that the newly synthesized PE and probably the active site of the enzyme are on the external leaflet of the membrane in all subfractions and that the ethanolamine base-exchange reaction has similar properties in all subfractions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1986.tb12946.x
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  • 2
    Electronic Resource
    Electronic Resource
    Sidedness of Phosphatidylcholine-Synthesizing Enzymes in Rat Brain Microsomal Vesicles (1985)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 44 (1985), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The sidedness of CDP-choline:1,2-diradylglycerol choline phosphotransferase (EC 2.7.8.2) and of the choline base-exchange activity has been studied in rat brain microsomal vesicles. Proteases (trypsin and pronase) and mercury-dextran have been used as reagents for membrane surface components. All of them could inactivate both enzymes to a good extent, without affecting the morphology or the permeability to sucrose of the vesicles. It is therefore concluded that CDP-choline:1,2-diradylglycerol choline phosphotransferase and the choline base-exchange activity are localized on the outer surface of rat brain microsomal vesicles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1985.tb07109.x
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  • 3
    Electronic Resource
    Electronic Resource
    Analysis of phospholipid molecular species (1997)
    Springer
    Molecular and cellular biochemistry 172 (1997), S. 129-136 
    Details
    ISSN: 1573-4919
    Keywords: phospholipid ; membranes ; diacylglycerol ; high performance liquid chromatography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract A method is described for analysing molecular species of glycerophospholipids. Diglycerides obtained by phospholipase C-catalysed hydrolysis of the phospholipid are separated into the diacyl- alkylacyl- and alkenylacyl- subclasses by HPLC on silicic acid. The molecular species of diacylglycerol are separated by HPLC of underivatised diglycerides on a reverse phase octadecyl-silica column.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006823806722
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  • 4
    Electronic Resource
    Electronic Resource
    Phospholipid base exchange enzyme activity in sarcolemmal membranes from the heart of cardiomyopathic hamsters (1992)
    Springer
    Molecular and cellular biochemistry 110 (1992), S. 47-54 
    Details
    ISSN: 1573-4919
    Keywords: cardiomyopathic hamsters ; base-exchange ; phospholipids ; sarcolemma ; heart
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The activity of phospholipid base exchange enzymes has been evaluated in cardiac sarcolemmal membranes from Syrian Golden hamsters and from a hamster strain (UM-X7.1) characterized by a genetic form of hypertrophic cardiomyopathy. No choline base exchange activity and only a little serine base exchange activity were detected, whereas the ethanolamine base exchange enzyme was found highly active in membranes from both strains. For this reason, the present study is focussed on the ethanolamine base exchange enzyme. The apparent Km for ethanolamine of ethanolamine base exchange enzyme from Syrian Golden membranes and from UM-X7.1 strain membranes are 18 and 32 µM, respectively. The specific activity of the sarcolemmal ethanolamine base exchange enzyme is lower in the UM-X7.1 strain than in Syrian Golden hamsters. The calcium-dependence of the enzyme appears different when the membranes from the two strains are compared. Indeed, after removal of the membrane-bound divalent cations, comparable activities are found in both membrane preparations, whereas, upon addition of Ca2+ to the incubation mixtures, the activity of the enzyme is enhanced in the membranes from Syrian Golden strain more than in those from UM-X7.1 strain. The cholesterol content of sarcolemmal membranes is higher in the cardiomyopathic strain than in the Syrian Golden hamsters. A possible relation between changes of the membrane lipid composition and of the ethanolamine base exchange activity is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02385005
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  • 5
    Electronic Resource
    Electronic Resource
    Kinetic changes of ethanolamine base exchange activity and increase of viscosity in sarcolemmal membranes of hamster heart during development of cardiomyopathy (1992)
    Springer
    Molecular and cellular biochemistry 116 (1992), S. 89-93 
    Details
    ISSN: 1573-4919
    Keywords: cardiomyopathic hamsters ; base-exchange ; phospholipids ; sarcolemma ; heart ; cholesterol ; fluidity
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The activity of the phospholipid base exchange enzyme specific for ethanolamine has been measured in cardiac sarcolemmal membrane preparations from Syrian golden and UM-X7.1 cardiomyopathic hamsters. In Syrian golden hamsters, the Km of the enzyme for ethanolamine does not change with age, whereas it almost doubles in membranes from cardiomyopathic animals, from the 30th to the 150th day of age. During the same period, the membrane cholesterol content increases by 68% in cardiomyopathic hamsters, whereas it does not change significantly in the Syrian golden hamster strain. As a consequence, in the adult animal, the cholesterol to phospholipid ratio and the viscosity of sarcolemmal membranes are higher in UM-X7.1 strain than in Syrian golden hamsters. A cause consequence relationship between the enzymatic changes and the compositional modifications in the sarcolemma occurring in UM-X7.1 hamsters during the development of cardiomyopahhy is proposed. (Mol Cell Biochem 116: 89–93,1992)
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01270574
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  • 6
    Electronic Resource
    Electronic Resource
    Quantitation of phospholipids on thin layer chromatographic plates using a desk-top scanner (1995)
    Springer
    Molecular and cellular biochemistry 145 (1995), S. 25-28 
    Details
    ISSN: 1573-4919
    Keywords: thin layer chromatography ; lipids ; phospholipids ; computer imaging ; photodensitometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Amethod for quantitating phospholipids separated on thin layer chromatographic plates by computer-assisted photodensitometry is described. After development, the plates are stained with molibdic reagent and the image obtained is acquired as TIFF file in the memory of a personal computer. The color intensity of the single spots of the digitalized image is analyzed using a dedicated software. Sensitivity and reproducibility are adequate for most of the needs of lipid chemist. When compared to conventional photodensitometric procedures, the present method offers the advantage of requiring a much cheaper hardware.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00925709
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  • 7
    Electronic Resource
    Electronic Resource
    Quantitation of glycerophosphorylcholine by flow injection analysis using immobilized enzymes (1996)
    Springer
    Molecular and cellular biochemistry 162 (1996), S. 83-87 
    Details
    ISSN: 1573-4919
    Keywords: flow injection analysis ; glycerophosphorylcholine ; glycerophosphorylethanolamine ; glycerophosphorylserine ; glycerophosphoric acid ; glycerophosphorylcholine-phosphodiesterase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract A method for quantitating glycerophosphorylcholine by flow injection analysis is reported in the present paper. Glycerophosphorylcholine phosphodiesterase and choline oxidase, immobilized on controlled porosity glass beads, are packed in a small reactor inserted in a flow injection manifold. When samples containing glycerophosphorylcholine are injected, glycerophosphorylcholine is hydrolyzed into choline and sn-glycerol-3-phosphate. The free choline produced in this reaction is oxidized to betain and hydrogen peroxide. Hydrogen peroxide is detected amperometrically. Quantitation of glycerophosphorylcholine in samples containing choline and phosphorylcholine is obtained inserting ahead of the reactor a small column packed with a mixed bed ion exchange resin. The time needed for each determination does not exceed one minute. The present method, applied to quantitate glycerophosphorylcholine in samples of seminal plasma, gave results comparable with those obtained using the standard enzymatic- spectrophotometric procedure. An alternative procedure, making use of co-immobilized glycerophosphorylcholine phosphodiesterase and glycerol-3-phosphate oxidase for quantitating glycerophosphorylcholine, glycerophosphorylethanolamine and glycerophosphorylserine is also described.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00227533
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  • 8
    Electronic Resource
    Electronic Resource
    Compartmentation of newly synthesized phosphatidylethanolamine in rat brain microsomes (1986)
    Springer
    The journal of membrane biology 90 (1986), S. 29-35 
    Details
    ISSN: 1432-1424
    Keywords: phosphatidylethanolamine ; cross-linking ; brain microsomes ; divalent cations
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Summary The compartmentation of the phosphatidylethanolamine newly synthesized in brain microsomesin vitro either by base exchange or net synthesis has been studied, using difluorodinitrobenzene as a chemical probe. The experimental results demonstrate that in rat brain microsomes the phosphatidylethanolamine molecules synthesized by base exchange and the bulk membrane lipid belong to different pools. Ca2+ bound to microsomes seems to be involved in the maintenance of the compartmentation of phosphatidylethanolamine. In the presence of Ca2+ the newly synthesized phosphatidylethanolamine molecules react with difluorodinitrobenzene as though they are organized in clusters. After biosynthesisin vivo orin vitro through the cytidine pathway, the compartmentation of the newly formed phosphatidylethanolamine appears less marked than after the synthesis through base exchange.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01869683
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  • 9
    Electronic Resource
    Electronic Resource
    Effect of various drugs producing convulsive seizures on rat brain glycerolipid metabolism (1985)
    Springer
    Neurochemical research 10 (1985), S. 879-885 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Convulsive seizures were elicited in the rat by the injection of several different drugs (pyridoxal phosphate, bicuculline, penicillin and ouabain). Glycerolipid metabolism was studied after the intraventricular injection of [2-3H]glycerol, which was incorporated into rat brain glycerides. The percentage of total lipid label found in each lipid class (phosphatidylethanolamine, PE; phosphatidylcholine, PC; phosphatidylserine, PS; phosphatidic acid, PA; phosphatidylinositol, PI; diacylglycerol (+ monoacylglycerol), DG and triacylglycerol, TG) depended on the time elapsed from the injection of the labeled precursor. The percent of total lipid radioactivity as PE and PC increased with time (3–60 min), whereas the opposite was true for the radioactivity of DG and PA. The radioactivity of other lipid classes did not appreciabily vary between 3 and 60 min from the injection of the labeled glycerol. The intraventricular administration of pyridoxal phosphate together with labeled glycerol decreased the percent of lipid radioactivity as PE and increased that as DG. This ‘lipid effect’ was detected also after the administration of other convulsants, such as ouabain and penicillin. The intraperitoneal administration of bicuculline affected lipid metabolism in cerebellum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00964625
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  • 10
    Electronic Resource
    Electronic Resource
    Uptake and utilization of CDP-choline in primary brain cell cultures from fetal brain (1983)
    Springer
    Neurochemical research 8 (1983), S. 333-340 
    Details
    ISSN: 1573-6903
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The utilization of double-labeled CDP-choline by cultured brain cells has been studied. CDP-choline is demonstrated to be rapidly hydrolysed into CMP and choline phosphate. The fragments, or their hydrolysis products, penetrate into the cells and are utilized for lipid synthesis. At short times after the isotope administration a rapid labeling of phosphatidylcholine was detected, when cells were incubated with CDP-choline. The same was not seen when cells were incubated with labeled choline. From these observations it can be inferred that either CDP-choline can penetrate the cell membrane or that some mechanism involving CDP-choline and leading to phospholipid synthesis can work at the external surface of the plasma membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00965723
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