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Results: 15101 to 15110 of 15112

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Comparative studies on highly metabolically active histone acetylation.
Moore M, Jackson V, Sealy L, Chalkley R
(1979) Biochim Biophys Acta 561: 248-60
MeSH Terms: Acetylation, Animals, Cell Cycle, Cell Division, Cell Line, Dactinomycin, Histone Deacetylases, Histones, Liver Neoplasms, Experimental, Mitosis, Neoplasm Proteins, Skin, Tetrahymena pyriformis, Thymus Gland
Show Abstract · Added March 5, 2014
Histone acetate is hydrolyzed rapidly in logarithmically dividing hepatoma tissue culture cells (Jackson, V., Shires, A., Chalkley, R. and Granner, D.K. (1975) J. Biol. Chem. 250, 4856--4863). The phenomenon has been analyzed further in hepatoma tissue culture cells at various stages of the cell cycle, in stationary phase, and in the presence of actinomycin D. We also investigated the phenomenon in Tetrahymena pyriformis macronuclei, bovine thymocytes, and human foreskin fibroblasts. The data suggest that this highly metabolically active histone acetylation while altered in mitotic cells, is independent of the overall rate of cell division, and is only slightly sensitive to actinomycin D. Finally, we conclude that the same general phenomenon is found in both cancerous and normal cells and is apparently common to cells from various stages of the evolutionary scale.
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14 MeSH Terms
Metabolism of thromboxane B2 in the monkey.
Roberts LJ, Sweetman BJ, Oates JA
(1978) J Biol Chem 253: 5305-18
MeSH Terms: Animals, Chromatography, Gas, Haplorhini, Male, Mass Spectrometry, Seminal Vesicles, Sheep, Thromboxane B2, Thromboxanes
Show Abstract · Added December 10, 2013
[3H8]Thromboxane B2 was biosynthesized and infused into an unanesthetized monkey. Several urinary metabolites were isolated and their structures elucidated using gas chromatography-mass spectrometry. In addition to the major urinary metabolite, dinor-thromboxane B2, a series of metabolites resulting from dehydrogenetion of the alcohol group at C-11 were identified: 11-dehydro-thromboxane B2, 11-dehydro-15-keto-13,14-dihydro-2,3-dinor-thromboxane B2, and 11-dehydro-15-keto-13,14-dihydro-19-carboxyl-2,3,4,5-tetranor-thromboxane B2. 6-(1,3-dihydroxypropyl)-7-hydroxy-10-oxo-3-pentadecaenoic acid was also identified. Three mono-O-ethylated metabolites were formed from thromboxane B2, which in this study was infused in an ethanolic solution. A small quantity of thromboxane B2 was excreted unchanged into the urine.
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9 MeSH Terms
Characterization of the specificity of DR monoclonal antibodies.
Molinaro GA, Quaranta V, Ferrone S
(1979) Transplant Proc 11: 1748-50
MeSH Terms: Animals, Antibody Specificity, B-Lymphocytes, Clone Cells, Cytotoxicity, Immunologic, Epitopes, HLA Antigens, Humans, Immune Sera, Immunoglobulin Fab Fragments, Mice, Mice, Inbred BALB C, Mice, Inbred NZB
Added March 27, 2014
1 Communities
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13 MeSH Terms
Lack of DR antigens on human B-lymphocyte-mouse fibroblast hybrids that express HLA-A,B antigens.
Glassy MC, Pellegrino MA, Quaranta V, Molinaro GA, Ferrone S
(1979) Transplant Proc 11: 1719-21
MeSH Terms: Animals, B-Lymphocytes, Cell Differentiation, Cell Line, Chromosomes, Human, 6-12 and X, Clone Cells, Epitopes, Fibroblasts, HLA Antigens, Humans, Hybrid Cells, Mice, Polymorphism, Genetic, Rabbits
Added March 27, 2014
1 Communities
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14 MeSH Terms
Site-specific anti-cytochrome c antibodies. Inhibition of the reactions between cytochrome c and its respiratory chain electron exchange partners.
Osheroff N, Jemmerson R, Speck SH, Ferguson-Miller S, Margoliash E
(1979) J Biol Chem 254: 12717-24
MeSH Terms: Animals, Antibodies, Antigen-Antibody Complex, Binding Sites, Antibody, Cytochrome c Group, Electron Transport, Epitopes, Horses, Immunoglobulin Fab Fragments, Kinetics, Models, Molecular, Protein Conformation, Rabbits
Added March 5, 2014
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13 MeSH Terms
Effects of indomethacin on cyclic nucleotide levels and histamine release from rat serosal mast cells.
Lewis RA, Holgate ST, Roberts LJ, Maguire JF, Oates JA, Austen KF
(1979) J Immunol 123: 1663-8
MeSH Terms: Animals, Arachidonic Acids, Cyclic AMP, Cyclic GMP, Epoprostenol, Histamine Release, Indomethacin, Mast Cells, Prostaglandins D, Rabbits, Rats
Added December 10, 2013
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11 MeSH Terms
Nitric oxide induced conformational changes in opossum hemoglobin.
John ME, Waterman MR
(1979) J Biol Chem 254: 11953-7
MeSH Terms: Amino Acids, Animals, Electron Spin Resonance Spectroscopy, Hemoglobin A, Hemoglobins, Humans, Hydrogen-Ion Concentration, Kinetics, Nitric Oxide, Opossums, Oxyhemoglobins, Protein Binding, Protein Conformation, Species Specificity
Show Abstract · Added February 12, 2015
Opossum hemoglobin assumes a T quaternary structure upon NO ligation in the absence of organic phophates at pH 6.7. In addition, stripped opossum hemoglobin exhibits a low oxygen affinity when compared to human hemoglobin and a pH-dependent heme-heme interaction with an n value of 2.14 at pH 7.0 and 2.46 at pH 7.35. These observations indicate that opossum hemoglobin may have a destabilized oxy structure when compared to hemoglobin A due to differences in primary structure. Thus, the strong trans ligand effect of nitric oxide is able to disrupt the proximal histidine-iron bond in the alpha-hemes triggering a conformational transition to the T state. Absence of a distal histidine in the alpha-subunits and, therefore an impaired donor acceptor interaction with the sixth ligand, could contribute to the lack of stability of the R quaternary structure in opossum nitrosylhemoglobin. The reduced oxygen affinity of opossum hemoglobin may be compensated for by other physiological factors such as a reduced phosphate effect.
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14 MeSH Terms
Phosphofructokinase. III. Correlation of the regulatory kinetic and molecular properties of the rabbit muscle enzyme.
Frieden C, Gilbert HR, Bock PE
(1976) J Biol Chem 251: 5644-7
MeSH Terms: Allosteric Regulation, Animals, Binding Sites, Enzyme Activation, Hydrogen-Ion Concentration, Kinetics, Muscles, Phosphofructokinase-1, Protein Binding, Rabbits, Temperature
Show Abstract · Added January 20, 2015
It is shown that the degree of regulatory kinetic behavior of rabbit muscle phosphofructokinase increases at a given pH and lower temperatures, as well as at a given temperature and lower pH values. It is also shown that the regulatory kinetic behavior which appears at lower pH values is inherent in the tetrameric (active) form of the enzyme. We conclude that a portion of the mechanism proposed previously (Bock, P.E., and Frieden, C. (1976) J. Biol. Chem. 251, 5630-5636) to describe the pH and temperature-dependent inactivation or reactivation may also be used to explain the pH and temperature-dependent regulatory kinetic behavior. According to this proposal, two rapidly equilibrating forms of the enzyme, which differ in the degree of protonation of specific residues, differ in their ability to bind substrates. While the protonated form of the enzyme subsequently becomes inactive by isomerization and dissociation, this process is too slow to affect the kinetic results, making direct comparisons between the association-dissociation behavior and regulatory kinetic behavior invalid. The time dependence of the processes of inactivation or reactivation in the presence or absence of ligands and of the appearance of regulatory kinetic behavior is discussed in relation to their possible role in metabolic regulation.
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11 MeSH Terms
Phosphofructokinase. II. Role of ligands in pH-dependent structural changes of the rabbit muscle enzyme.
Bock PE, Frieden C
(1976) J Biol Chem 251: 5637-43
MeSH Terms: Adenosine Triphosphate, Animals, Binding Sites, Enzyme Activation, Hydrogen-Ion Concentration, Inosine Nucleotides, Kinetics, Ligands, Magnesium, Muscles, Phosphofructokinase-1, Protein Binding, Protein Conformation, Rabbits
Show Abstract · Added January 20, 2015
The effect of ligands, including substrates and allosteric effectors, on the pH-dependent inactivation and reactivation of rabbit muscle phosphofructokinase has been examined in terms of the mechanism proposed previously (Bock, P.E. and Fireden, C. (1976) J. Biol. Chem. 251, 5630-5636). It is concluded thatt many ligands exert their effect by binding preferentially to either protonated or unprotonated forms of the enzyme and thus shifting an apparent pK for the inactivation or reactivation process. ATP and fructose 6-phosphate influence the apparent pK to different extents and in different directions, with ATP binding preferentially to the protonated forms and fructose 6-phosphate to the unprotonated forms. Enzyme inactivated by ATP can be reactivated by the addition of fructose 6-phosphate. The experiments indicate that inactivation and reactivation in the presence of these ligands can occur by kinetically different pathways as has been found for these processes in the absence of ligands. The results are discussed in relation to what might be expected for ligand binding properties of the enzyme as a function of pH, temperature, and enzyme concentration. The effect of ATP and MgATP is complex, perhaps representing more than one site of binding. Citrate appears to bind preferentially to protonated forms of the enzyme while fructose 1,6-bisphosphate and AMP bind preferentially to the unprotonated forms. ADP, K+, and NH4+ appear to have little or no preference in binding to different enzyme forms.
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14 MeSH Terms
Phosphofructokinase. I. Mechanism of the pH-dependent inactivation and reactivation of the rabbit muscle enzyme.
Bock PE, Frieden C
(1976) J Biol Chem 251: 5630-6
MeSH Terms: Animals, Enzyme Activation, Hydrogen-Ion Concentration, Kinetics, Muscles, Phosphofructokinase-1, Rabbits, Temperature
Show Abstract · Added January 20, 2015
The kinetics of inactivation and reactivation of rabbit skeletal muscle phosphofructokinase have been studied as a function of pH and enzyme concentration at constant temperature in phosphate buffer. From the enzyme concentration dependence, we conclude that the minimal mechanism for inactivation involves a protonation step followed by isomerization to an inactive form and then dissociation to a species of one-half the molecular weight. Other data indicate a subsequent isomerization of the dissociated form. The pH and temperature dependence of the inactivation process shows that it is controlled by ionizable groups, and that the apparent pK for these groups is temperature-dependent in such a way as to make the enzyme show the characteristic of cold lability below pH 7. Reactivation of the inactive enzyme occurs by a kinetically different pathway involving deprotonation of an inactive, dissociated form to a form which may either isomerize to another inactive form, or dimerize to the active enzyme. A general mechanism is postulated in which the inactivation and reactivation processes are different aspects of the same mechanism. This mechanism assumes four species (two containing four subunits and two containing two subunits) each of which can exist in a protonated and unprotonated form. Inactivation or reactivation induced by changes in pH or temperature reflect the kinetic establishment of a new steady state between these forms. How the apparent pK values which control the distribution of the enzyme between protonated and unprotonated forms describe the pH-dependent characteristics of the enzyme is discussed in terms of the proposed mechanism.
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8 MeSH Terms