Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027960 (mole)
 21,279 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The interaction of 3H-GABA (gamma-aminobutyric acid and 14C-glutamate with lipids in an aqueous organic partition system was studied. With this partition system 3H-GABA and 14C-glutamate were able to interact with sphingomyelin, sulfatide, phosphatidylcholine, phosphatidylserine, phosphatidylethanolamine and phosphatidic acid but not with cholesterol or ceramide. In an homogeneous aqueous medium we could not demonstrate any interaction between 3H-GABA and lipids. The apparent dissociation constants (Kd) for 3H-GABA-lipids or 14C-glutamate-lipids interactions in organic medium were in the millimolar range and maximal charge (Bmax) between 3 and 7 moles of GABA or glutamate by mole of lipid. Amino acids such as glutamic acid, beta-alanine and glycine displaced 3H-GABA with the same potency as GABA itself; thus these results show that the interaction lacks pharmacological specificity. To detect this interaction lipid concentrations higher than 2 microM were required and in the partition system 3H-GABA and lipid phosphorus were both concentrated at the interface. Therefore lipids tested with a biphasic partition system do not fulfill the classical criteria for a neurotransmitter receptor at least not for GABA and glutamate.
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PMID:GABA interaction with lipids in organic medium. 288 73

We measured brain energy phosphate metabolism and intracellular pH (pHi) in a cross-sectional study of migraine patients by in vivo phosphorus 31 NMR spectroscopy. During a migraine attack the ratio ATP/total phosphate signal (mole % ATP) was preserved, but there was a decrease in mole % phosphocreatine (PCr) and an increase in mole % inorganic phosphate (Pi) resulting in a decrease of the PCr/Pi ratio, an index of brain phosphorylation potential. This was found in classic but not common migraine. Mole % Pi was also increased in combined brain regions between attacks. There was no alteration in brain pHi during or between attacks. Energy phosphate metabolism but not pHi appears disordered during a migraine attack.
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PMID:Preliminary observations on brain energy metabolism in migraine studied by in vivo phosphorus 31 NMR spectroscopy. 292 79

The phospholipid and fatty acid contents of developing rod photoreceptor cells were determined in dissociated photoreceptor cells obtained from normal mice and from rd mice exhibiting an inherited retinal degeneration. Photoreceptors were dissociated from retinas by mechanical agitation after mild protease treatment and characterized by light and electron microscopy. Phospholipid classes were isolated by thin-layer chromatography, and fatty acyl groups separated and quantitated by capillary gas-liquid chromatography. Developing photoreceptor cells of normal retinas accumulated all phospholipid classes, but in proportions which shifted with age. The mole % contents of phosphatidylcholine (PC) and phosphatidylinositol (PI) decreased with age, whereas phosphatidylethanolamine (PE) and phosphatidylserine (PS) increased. The content of the polyunsaturated fatty acid docosahexaenoate (22:6), expressed as nmol/microgram lipid phosphorus, increased rapidly during development, whereas arachidonate (20:4) content tended to decline. Mono-unsaturated fatty acid levels (palmitoleate, 16:1; oleate, 18:1) declined with age. Among saturated fatty acids, palmitate (16:0) decreased during normal development, whereas stearate (18:0) increased. The total mass of phospholipid/photoreceptor cell in the normal, adult mouse retina was estimated to be approximately 14 pg. The total phospholipid content and mole % distribution of individual phospholipid classes in immature rd photoreceptors were similar to values for normal cells. In contrast, significant changes in fatty acid composition were detected between immature rd cells and normal cells. Rd cells generally had higher levels of saturated (myristate, 14:0; palmitate, 16:0) and monounsaturated fatty acids (oleate, 18:1) and lower levels of polyunsaturated fatty acids (arachidonate, 20:4; docosahexaenoate, 22:6), suggesting that fatty acid metabolism is altered by expression of the rd gene and/or by the associated impairment of photoreceptor cell differentiation.
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PMID:Developing rod photoreceptors from normal and mutant Rd mouse retinas: altered fatty acid composition early in development of the mutant. 317 77

A 107 kDa (pp107) casein kinase G (ck-G) substrate has been purified from mouse and beef thyroid cytosol; ck-G was purified from beef thyroid cytosol. Ck-G and pp107 were found to co-elute on DEAE cellulose chromatography at approximately 300 mM NaCl. Ck-G and pp107 were separated by spermine-agarose affinity chromatography; pp107 is eluted with a stepped gradient at 250 mM NaCl and ck-G is eluted at 500 mM NaCl. Ck-G was subsequently purified by casein-agarose and GTP-agarose affinity chromatography. The 107 kDa protein was purified using heparin-agarose affinity chromatography. Phosphorylation of purified pp107 by ck-G was stimulated by spermine (ED50 = 0.2 mM) and inhibited by low concentrations of heparin (0.1-5 micrograms/ml). The Km and Vmax for the reaction were 1.46 microM and 32.2 nmoles P transferred/20 min/mg protein, respectively; 1 mole pp107 incorporated 0.81 mole phosphorus. pp107 was found to be an acidic substrate with a pI of 3.87 and was absorbed to wheat-germ agglutinin-agarose. The specificity of pp107 phosphorylation was studied using diacylglycerol-activated calcium/phospholipid-dependent protein kinase C, calcium-activated calmodulin-dependent protein kinase, and the catalytic subunit of cAMP-dependent protein kinase A. Phosphorylation of pp107 by the other protein kinases tested never exceeded 4% of that of ck-G. Our data show that pp107 is an acidic glycoprotein which may serve as a high-affinity and specific substrate for ck-G.
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PMID:Purification of a 107 kilodalton (kDa) casein kinase G substrate from thyroid cytosol. 320 Feb 52

Phosphorus 31 magnetic resonance spectroscopy (31P MRS) was used to study noninvasively the intracellular free Mg2+ concentration and cellular bioenergetic state of rat brain in vivo before and after fluid percussion-induced traumatic brain injury of graded severity. Brain injury was induced at four levels: low (1.0 +/- 0.5 atm); moderate (2.1 +/- 0.4 atm); high (3.9 +/- 0.9 atm); and severe (5.9 +/- 0.7 atm). Prior to injury, mean intracellular values for all groups (n = 24; mean +/- SE) were as follows: pH = 7.11 +/- 0.03; free [Mg2+] = 0.99 +/- 0.07 mM; cytosolic [ADP] = 25.2 +/- 0.8 nmol/g wet weight; cytosolic [AMP] = 0.29 +/- 0.02 nmol/g wet weight; cytosolic phosphorylation potential = 118.5 +/- 3.1 X 10(3) M-1; free energy of ATP hydrolysis = 62.11 +/- 0.04 kJ/mole; and energy charge = 0.99 +/- 0.01. Following every level of injury, there were decreases in intracellular free Mg2+ concentration, and alterations in the intracellular pH. These posttraumatic changes in Mg2+ and pH induced shifts in the equilibrium constants of the creatine kinase, adenylate kinase, and ATPase reactions, resulting in alterations in [ADP], [AMP], cytosolic phosphorylation potential, and free energy of hydrolysis, but not in the energy charge. The alterations in cytosolic phosphorylation potential following trauma were linearly correlated with the changes in intracellular free Mg2+ concentration. None of the individual bioenergetic parameters could be correlated with the severity of injury over the entire injury range; however, an association between cytosolic phosphorylation potential and reversibility of injury was apparent. These results suggest that reductions in cellular bioenergetic state following traumatic brain injury occur through a posttraumatic decrease in the cells' capacity for oxidative phosphorylation, which itself may be directly related to the intracellular free Mg2+ concentration.
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PMID:Changes in cellular bioenergetic state following graded traumatic brain injury in rats: determination by phosphorus 31 magnetic resonance spectroscopy. 324 10

Bovine myelin proteolipid apoprotein (PLA), obtained in high yield and purity by a novel ultrafiltration procedure, has been used to study the perturbations produced by this protein on phosphatidylcholine bilayers, using infrared spectroscopy, nuclear magnetic resonance and fluorescence polarisation. PLA interacts with phospholipids in a similar manner to other intrinsic proteins. For bilayers in the fluid state, the fatty-acyl chain static order, as measured by deuterium NMR, is slightly increased in the presence of the protein, except at very high PLA concentrations. Phosphorus NMR reveals some perturbation of the phospholipid polar group by PLA, but to a smaller degree than occurs with other intrinsic proteins. An increase in static order above tc (the onset temperature for gel-to-fluid transition) is also detected by infrared spectroscopy. Studies using steady-state polarisation of diphenylhexatriene fluorescence indicate that the microviscosity of the bilayer increases as a function of the protein mole fraction. From these data an estimation of the average number of lipids perturbed per protein monomer has been made, and a figure of 37 phospholipid molecules determined. The data are compatible with a picture of a hydrophobic polypeptide, perturbing the phospholipids close to it, but allowing rapid (greater than 10(4) s-1) exchange with all the lipid molecules in the system.
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PMID:Lipid-protein interaction. The incorporation of myelin proteolipid apoprotein into phosphatidylcholine bilayers. 339 Nov 75

Cytochrome o(561,564) terminal oxidase was solubilized from the membrane fraction of the bacterium Vitreoscilla sp., strain C1, and purified by differential pH dialysis, gel filtration chromatography, and ion-exchange chromatography. Subunit molecular weights, determined on sodium dodecyl sulfate-polyacrylamide gels by the Ferguson plot method, were 49,500 and 23,500. There were two protohemes IX, two coppers, and 45 mol of phosphorus per mole of protomer (73,000). The molecular weight of the cytochrome o complex estimated by chromatography on Sephacryl-400 in deoxycholate was 265,000, which is consistent with the enzyme complex under these conditions being a dimer (146,000) with the remaining molecular weight contribution arising from bound phospholipid, deoxycholate, and possibly other, smaller subunits. Difference spectra of the dithionite-reduced enzyme have split alpha absorption maxima at 561 and 564 nm at room temperature and 558 and 561 nm at 77 K. The CO difference spectrum at room temperature has absorption maxima at 570, 534, and 416 nm. Dissociation constants for CO and cyanide binding to the reduced and oxidized forms of the oxidase are 5.2 microM and 3.5 mM, respectively. The hemes in the cytochrome are one electron accepting centers, both with midpoint potentials around +165 mV at pH 7.0. The enzyme is highly autoxidizable, and its menadiol oxidizing activity is stimulated by phospholipids.
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PMID:Purification and partial characterization of the membrane-bound cytochrome o(561,564) from Vitreoscilla. 342 21

This and two accompanying reports describe the intrinsic binding energy derived from a single hydrogen bond between an inhibitor and an enzyme. The results were obtained by comparing matched pairs of inhibitors of the zinc endopeptidase thermolysin that bind to the enzyme in an essentially identical manner but differ in the presence or absence of a specific hydrogen bond. This report describes five phosphorus-containing analogs of the peptides carbobenzoxy-Gly-Leu-X, in which the Gly-Leu peptide linkage is replaced with a phosphonate ester (-PO2(-)-O-). Values for the inhibition constants of these inhibitors show a direct relation with those of the corresponding phosphonamidate analogs (-PO2(-)-NH- in place of the Gly-Leu peptide moiety), which have been characterized previously as transition state analogs. However, each phosphonate ester is bound about 840 times more weakly than the analogous phosphonamidate, reflecting the loss of 4.0 +/- 0.1 kilocalories per mole in binding energy. From these results and the crystallographic analysis in the next report, it can be inferred that the value of 4.0 kilocalories per mole represents the intrinsic binding energy arising from a highly specific hydrogen binding interaction.
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PMID:Evaluation of intrinsic binding energy from a hydrogen bonding group in an enzyme inhibitor. 381 Jan 55

The preparation of cytoplasmic membranes from suspensions of Staphylococcus aureus lysed by an enzyme recently isolated in these laboratories is described. These membranes contained: protein, 34.4%; ribonucleic acid, 6.6%; lipids, 34.5%; and total phosphorus, 1.4%. Such membranes exhibited adenosine 5'-triphosphatase (E.C. 3.6.1.3) activity, liberating orthophosphate at an initial rate of 0.53 mumole per min per mg of protein under optimal conditions. The enzyme was Mg(++)-dependent and K(+)- or Na(+)-stimulated. Maximal activity was observed with a molar adenosine 5'-triphosphate (ATP) to Mg(++) ratio of 1. One mole of orthophosphate was liberated per mole of ATP; the other product of digestion was adenosine 5'-diphosphate. Inorganic pyrophosphate and the 5'-triphosphates of guanosine, uridine, and cytidine were also attacked by membrane preparations, but more slowly than ATP. Ouabain, p-chloromercuribenzoate, and 2,4-dinitrophenol did not alter adenosine triphosphatase activity, whereas both Atebrine and chlorpromazine were inhibitory.
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PMID:Adenosine triphosphatase in isolated membranes of Staphylococcus aureus. 423 Aug 57

1. The lipids of Bacillus megaterium were extracted and three lipids containing glucosamine were identified. One of these is not a phospholipid, but the other two, which differ in their chromatographic behaviour, contain phosphorus, glycerol, fatty acid and d-glucosamine in the molar proportions 1:2:2:1. 2. In both phosphoglycolipids, the fatty acids are bound in ester linkage, and both yield 2,5-anhydromannose and 3-sn-phosphatidyl-1'-sn-glycerol on treatment with sodium nitrite. 3. Both phosphoglycolipids were N-acetylated and, after removal of fatty acids by mild alkaline hydrolysis, in both cases N-acetylglucosamine was quantitatively released by beta-N-acetylhexosaminidase. 4. The glucosaminylglycerols derived from the two phosphoglycolipids by partial acid hydrolysis differ in their behaviour towards periodate. In one case 1 mole of periodate is rapidly consumed/mole of glucosaminylglycerol, but in the other case under identical conditions the consumption of periodate is negligible. 5. The phosphoglycolipids were identified as 1'-(1,2-diacyl-sn-glycero-3-phosphoryl)-3'-O-beta-(2-amino-2-deoxy-d-glucopyranosyl)-sn-glycerol and as 1'-(1,2-diacyl-sn-glycero-3-phosphoryl)-2'-O-beta-(2-amino-2-deoxy-d-glucopyranosyl)-sn-glycerol. 6. Both phosphoglycolipids are good substrates for phospholipase A: neither is a substrate for phospholipase C from Clostridium perfringens, and only the 3'-glucosaminide is a substrate for phospholipase D.
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PMID:Isomers of glucosaminylphospatiylglycerol in Bacillus megaterium. 430 9


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