Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rat thymocytes were exposed in vitro to the corticosteroid dexamethasone, 10 nM, for 10 min, or to oleic acid, 500 nM for 2 min. This results in cytolysis after 6 hr, if incubation is continued. Instead, the cells were centrifuged, the supernatant fluid decanted, and the cells subjected to osmotic shock in 1.5 mM MgCl2. The naked nuclei were incubated at 37 degrees C and examined by light and electron microscopy. Nuclear edema was evident early, and most nuclei showed damage with variation in shape and size and distinct folds, which was maximal by 1-2 hr as a result of these treatments. This was true also if nuclei were incubated in MgF2 or Mg(NO3)2 but not in MgBr2, MgI2, MgSO4 or Mg-citrate. Spleen lymphocyte nuclei showed similar damage but only after incubation with 20 microM oleic acid, and not at all with corticosteroids. The effects of both steroid and fatty acid, even at greatly increased concentrations, were inhibited by tri-n-butyl tin chloride, 10 microM, and by 4-4'-diisothiocyanostilbene-2,2'-disulfonic acid, sodium salt, 10 microM, both of which block chloride ion transport. It is concluded that the cytolytic effects of both corticosteroids and free fatty acids involve influx of chloride ion resulting in nuclear edema, which subsequently leads to fragmentation of chromatin, karyorrhexis and, ultimately, cytolysis.
Mol Cell Biochem 1984 Sep
PMID:Role of anions in the lymphocytolytic action of corticosteroids and fatty acids. 649 16

The DNA helix-coil transition in nonbuffer solutions of Fe(NO3)3 was studied. Calculation of the ionic equilibrium indicated that in these solutions iron exists in the form of mono-, bi- or trivalent hydroxide, the formation of which decreases pH. A component of the DNA thermal stability variation associated with DNA binding to iron ions was calculated. An increase in the iron contents produces an increase in the melting range which was determined by a rise in the melting end temperature when binding the ions with phosphates and a drop in the melting beginning temperature when binding to DNA bases. A main contribution to the former effect is made by [Fe2(OH)3]3+ ions and to the latter effect by [FeOH]2+ ions. The constants of ion binding are higher for bases than for phosphates. Differential UV spectra of native and denatured DNA due to iron ions were measured. Calculations of conformation and coordination components of these spectra show that G-C pairs are one of the possible sites of iron ion binding with DNA.
Mol Biol (Mosk)
PMID:[Binding of ions of trivalent iron with DNA]. 662 27

Assimilatory nitrate reductase (NAD(P)H-nitrate oxidoreductase, EC 1.6.6.2) from the green alga Ankistrodesmus braunii can be purified to homogeneity by dye-ligand chromatography on blue-Sepharose. The purified enzyme, whose turnover number is 623 s-1, presents an optimum pH of 7.5 and Km values of 13 microM, 23 microM and 0.15 mM for NADH, NADPH and nitrate, respectively. The NADH-nitrate reductase activity exhibits an iso ping pong bi bi kinetic mechanism. The molecular weight of the native nitrate reductase is 467 400, while that of its subunits is 58 750. These values suggest an octameric structure for the enzyme, which has been confirmed by electron microscopy. As deduced from spectrophotometric and fluorimetric studies, the enzyme contains FAD and cytochrome b-557 as prosthetic groups. FAD is not covalently bound to the protein and is easily dissociated in diluted solutions from the enzyme. Its apparent Km value is 4 nM, indicative of a high affinity of the enzyme for FAD. The results of the quantitative analyses of prosthetic groups indicate that nitrate reductase contains four molecules of flavin, four heme irons, and two atoms of molybdenum. The three components act sequentially transferring electrons from reduced pyridine nucleotides to nitrate, thus forming a short electron transport chain along the protein. A mechanism is proposed for the redox interconversion of the nitrate reductase activity. Inactivation seems to occur by formation of a stable complex of reduced enzyme with cyanide or superoxide, while reactivation is a consequence of reoxidation of the inactive enzyme. Both reactions imply the transfer of only one electron.
Mol Cell Biochem 1983
PMID:Assimilatory nitrate reductase from the green alga Ankistrodesmus braunii. 668 79

Introduction of chlA, B or E mutant alleles into strains carrying fusions between the lac structural genes and the promoter of the nitrate reductase operon led to the partial or total constitutive expression of the fusion. Presence of chlD mutated alleles in the same strains did not result in constitutive expression of the fusion and allowed full induction by nitrate only in the presence of molybdenum. It is proposed that the molybdenum cofactor, Mo-X, of the nitrate reductase is also corepressor of the operon. The chlA, B and E genes would be involved in the biosynthesis of the X-moity. Mutations in these genes would give an altered X-moity which still binds to molybdenum but leads to a less efficient repressor complex; chlD gene would code for an enzyme inserting molybdenum in the X-moity of the cofactor. Mutations in chlD give an empty cofactor leading to a complex which permanently represses the operon unless molybdenum is added.
Mol Gen Genet 1982
PMID:Regulation of the nitrate reductase operon: effect of mutations in chlA, B, D and E genes. 675 67

The wild-type heterocystous and nitrogen-fixing (Het+Nif+) N. muscorum and its non-heterocystous non-nitrogen-fixing (Het-Nif-) mutant strain both fail to grow in different inorganic nitrogen media containing 1 mM methylamine hydrochloride (MA). Mutants of the Het+Nif+ and Het-Nif- parents resistant to growth inhibition by 5 mM MA and thus designated as MAR strains were isolated with a frequency of 2.5(+/- 2.4) x 10(6). A MAR strain of the Het+Nif+ and a MAR strain of the Het-Nif- parent were characterized for growth, heterocyst formation and acetylene reducing activity in the presence and absence of methylamine in N2 medium. The Het+Nif+ MAR strain grows better in MA containing than in MA-free N2 medium, and all cultures grown with MA are found to lack both acetylene reducing activity and heterocyst. The Het-Nif-MAR strain shows good growth in MA-containing N2 medium but no growth in MA-free N2 medium. Furthermore, both the Het+Nif+MAR and Het-Nif-MAR strains show better growth in the presence than in the absence of MA in NO3- and HN4+ media. These results appear to suggest that the MAR phenotype in N. muscorum is due to the metabolic utilization of the ammonium analog as a nitrogen source.
Mol Gen Genet 1981
PMID:Isolation and preliminary characterization of mutants of the cyanobacterium Nostoc muscorum resistant to growth inhibition by methylamine. 679 49

Six mutant strains (301, 102, 203, 104, 305, and 307) affected in their nitrate assimilation capability and their corresponding parental wild-type strains (6145c and 21gr) from Chlamydomonas reinhardii have been studied on different nitrogen sources with respect to NAD(P)H-nitrate reductase and its associated activities (NAD(P)H-cytochrome c reductase and reduced benzyl viologen-nitrate reductase) and to nitrite reductase activity. The mutant strains lack NAD(P)H-nitrate reductase activity in all the nitrogen sources. Mutants 301, 102, 104, and 307 have only NAD(P)H-cytochrome c reductase activity whereas mutant 305 solely has reduced benzyl viologen-nitrate reductase activity. Both activities are repressible by ammonia but, in contrast to the nitrate reductase complex of wild-type strains, require neither nitrate nor nitrite for their induction. Moreover, the enzyme from mutant 305 is always obtained in active form whereas nitrate reductase from wild-types needs to be reactivated previously with ferricyanide to be fully detected. Wild-type strains and mutants 301, 102, 104, and 307, when properly induced, exhibit an NAD(P)H-cytochrome c reductase distinguishable electrophoretically from constitutive diaphorases as a rapidly migrating band. Nitrite reductase from wild-type and mutant strains is also repressible by ammonia and does not require nitrate or nitrite for its synthesis. These facts are explained in terms of a regulation of nitrate reductase synthesis by the enzyme itself.
Mol Gen Genet 1982
PMID:Regulation of the nitrate-reducing system enzymes in wild-type and mutant strains of Chlamydomonas reinhardii. 681 63

The existence of a nitrate-reductase operon in the tryptophane region was deduced from the effects of prophage insertion in each of chlI and chlC genes and from transposition of the Mu-mediated host DNA fragments of F-prime. This operon appears to be polarized from chlC to chlI and the gene order in the region is trp -- chlI -- chlC -- purB.
Mol Gen Genet 1981
PMID:Nitrate reductase and cytochrome bnitrate reductase structural genes as parts of the nitrate reductase operon. 702 29

The hypothesis stating that chloroplasts were derived from a photosynthetic procaryote is explored at a genetic and biochemical level. A transfer of genetic material from the endosymbiont to the nucleus of the host cell is proposed along with a corollary argument that the protein products of such transferred genes have remained specific to the chloroplast. This model provides an explanation for the presence of plastid-specific isozymes which are coded by nuclear DNA. It also suggests that the genome of the endosymbiont contributed the information necessary for the biosynthesis of carotenoids and the "essential" amino acids and the assimilation of nitrate-nitrogen and sulfate-sulfur. Animal cells lack these capabilities not because such were lost subsequent to the divergence of the plant and animal lines, but because animal cells did not become host to the appropriate symbionts. Additional implications of this thesis are discussed.
J Mol Evol 1981
PMID:Genetic and biochemical implications of the endosymbiotic origin of the chloroplast. 726 65

The effects of ions on the interaction of lac repressor protein and operator DNA have been studied by the membrane filter technique. The equilibrium association constant was determined as a function of monovalent and divalent cation concentrations, anions, and pH. The binding of repressor and operator is extremely sensitive to the ionic environment. The dependence of the observed equilibrium constant on salt concentration is analyzed according to the binding theory of Record et al. [Record, M. T., Jr., Lohman, T. M., & deHaseth, P. L. (1976) J. Mol. Biol. 107, 145]. The number of ionic interactions in repressor--operator complex is deduced from the slopes of the linear log-log plots. About 11 ionic interactions are formed between repressor and DNA phosphates at pH 7.4 and about 9 ionic interactions at pH 8.0, in reasonable agreement with previous estimates. A favorable nonelectrostatic binding free energy of about 9-12 kcal/mol is estimated from the extrapolated equilibrium constants at the 1 M standard state. The values are in good accord with recent results for the salt-independent binding of repressor core and operator DNA. The effects of pH on the repressor--operator interaction are small, and probably result from titration of functional groups in the DNA-binding site of the protein. For monovalent salts, the equilibrium constant is slightly dependent on cation type and highly dependent on anion type. At constant salt concentration, the equilibrium constant decreases about 10000-fold in the order CH3CO2- greater than or equal to F- greater than Cl- greater than Br- greater than NO3- greater than SCN- greater than I-. The wide range of accessible equilibrium constants provides a useful tool for in vitro studies of the repressor--operator interaction.
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PMID:Ion effects on the lac repressor--operator equilibrium. 727 80

The effects of L-arginine on recovery of myocardial contractile function and oxidative metabolism were investigated in a model of reversible global normothermic, ischemic injury using an isolated, buffer-perfused rabbit heart preparation. One mM L-arginine was infused into hearts for 2 min at the onset (group 1) of a 35 min period of ischemia or at the onset of reperfusion (group 2). In non-ischemic hearts, L-arginine caused a slight increase in developed pressure but had no effects on diastolic pressure, oxygen consumption (MVO2), coronary flow, or lactate production. When administered either before or after ischemia-reperfusion. L-arginine caused a significant increase in the diastolic pressure-volume relationship (PVR) and decline in systolic function when compared to untreated control hearts receiving the same ischemic injury. Recovery of MVO2 and high energy phosphates (phosphocreatine and ATP), measured by 31P-NMR spectroscopy, were significantly impaired in L-arginine-treated hearts compared to reperfused control hearts. Lactate release on reperfusion was also higher in both arginine-treated groups. Nitric oxide release into the coronary circulation (measured in separate experiments by the conversion of [15N]L-arginine to [15N]nitrate/nitrite using gas chromatography/mass spectroscopy) was not increased by L-arginine administration. Thus, we conclude that L-arginine acts synergistically with ischemia reperfusion to augment myocardial injury, which includes inhibition of oxidative metabolism and mitochondrial function.
J Mol Cell Cardiol 1995 Jul
PMID:Direct detrimental effects of L-arginine upon ischemia--reperfusion injury to myocardium. 747 86


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