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Results: 101 to 105 of 105

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Regulation of tryptophan pyrrolase activity in Xanthomonas pruni.
Wagner C, Brown AT
(1970) J Bacteriol 104: 90-7
MeSH Terms: Ascorbic Acid, Heme, Kinetics, Kynurenine, Niacinamide, Nicotinic Acids, Porphyrins, Tryptophan Oxygenase, Xanthomonas, ortho-Aminobenzoates
Show Abstract · Added January 20, 2015
Tryptophan pyrrolase was studied in partially purified extracts of Xanthomonas pruni. The dialyzed enzyme required both heme and ascorbate for maximal activity. Other reducing agents were able to substitute for ascorbate. Protoporphyrin competed with heme for the enzyme, suggesting that the native enzyme is a hemoprotein. The enzyme exhibited sigmoid saturation kinetics. Reduced nicotinamide adenine dinucleotide (NADH), reduced nicotinamide adenine dinucleotide phosphate (NADPH), nicotinic acid mononucleotide, and anthranilic acid enhanced the sigmoid kinetics and presumably bound to allosteric sites on the enzyme. The sigmoid kinetics were diminished in the presence of alpha-methyltryptophan. NAD, NADP, nicotinic acid, nicotinamide, nicotinamide mononucleotide, and several other related compounds were without effect on the activity of the enzyme. These data indicate that the activity of the enzyme is under feedback regulation by the ultimate end products of the pathway leading to NAD biosynthesis, as well as by certain intermediates of this pathway.
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10 MeSH Terms
Deduced amino acid sequence of heme binding region of chicken cholesterol side chain cleavage cytochrome P450.
Mathew PA, Kagawa N, Bhasker CR, Waterman MR
(1990) Protein Seq Data Anal 3: 323-5
MeSH Terms: Amino Acid Sequence, Animals, Base Sequence, Binding Sites, Chickens, Cholesterol, Cholesterol Side-Chain Cleavage Enzyme, Heme, Humans, Molecular Sequence Data, Restriction Mapping, Sequence Homology, Nucleic Acid
Show Abstract · Added February 12, 2015
The primary structure of the carboxy terminal 296 amino acids of chicken cholesterol side chain cleavage cytochrome P450 (P450scc) was deduced from a partial cDNA clone isolated from a chicken ovarian cDNA library. The sequence contained putative steroid binding and heme binding regions. Comparison of this sequence with the corresponding sequences of three mammalian forms of P450scc shows greater than 50% homology. The heme binding region of the avian P450scc shows 76% homology with the heme binding regions of rat and human P450scc and 81% homology with that of bovine P450scc.
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12 MeSH Terms
The hydrophobic amino-terminal sequence of bovine 17 alpha-hydroxylase is required for the expression of a functional hemoprotein in COS 1 cells.
Clark BJ, Waterman MR
(1991) J Biol Chem 266: 5898-904
MeSH Terms: Amino Acid Sequence, Animals, Base Sequence, Blotting, Western, Cattle, Cell Fractionation, Cell Line, Endoplasmic Reticulum, Gene Expression Regulation, Enzymologic, Hemeproteins, Molecular Sequence Data, Steroid 17-alpha-Hydroxylase, Transfection
Show Abstract · Added February 12, 2015
The endoplasmic reticulum is a major site of localization for eukaryotic cytochrome P-450 mixed-function oxidase complexes. Previous studies have shown that the microsomal forms of P-450 insert into the membrane via their hydrophobic amino terminus through the signal recognition particle-dependent pathway. We have examined the insertion of bovine 17 alpha-hydroxylase (P45017 alpha) into the endoplasmic reticulum of COS 1 cells to evaluate the functional role of its hydrophobic amino-terminal sequence and membrane insertion. An NH2-terminal truncated protein, P450 delta 2-17, which lacked amino acids 2-17 was expressed in COS 1 cells, subcellular fractions were isolated, and P450 delta 2-17 was localized by immunoblot analysis. Compared to the full-length P45017 alpha, the NH2-terminal truncation resulted in a 2.5-fold decrease in P45017 alpha protein recovered with the microsomal fraction, 50% of which was an integral membrane protein as defined by resistance to Na2CO3 extraction. Despite correct membrane localization, P450 delta 2-17 was not a functional enzyme in COS 1 cells. A CO difference spectrum of microsomes containing P450 delta 2-17 did not give a typical 450 nm absorbance. We conclude that the hydrophobic amino terminus is required for the expression of a functionally competent P45017 alpha in COS 1 cells and suggest that the insertion of the amino terminus into the membrane is necessary for the folding of this protein into its correct structural form.
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13 MeSH Terms
Enhancement of heme oxygenase-1 synthesis by glutathione depletion in Chinese hamster ovary cells.
Saunders EL, Maines MD, Meredith MJ, Freeman ML
(1991) Arch Biochem Biophys 288: 368-73
MeSH Terms: Animals, Antimetabolites, Blotting, Western, Buthionine Sulfoximine, Cadmium, Cadmium Chloride, Cell Line, Cricetinae, Cricetulus, Electrophoresis, Gel, Two-Dimensional, Electrophoresis, Polyacrylamide Gel, Female, Glutathione, Heat-Shock Proteins, Heme Oxygenase (Decyclizing), Kinetics, Maleates, Methionine Sulfoximine, Molecular Weight, Ovary
Show Abstract · Added March 5, 2014
Chinese hamster ovary cells cultured in vitro were used to assess the role of glutathione metabolism in the induction of the 32-kDa stress protein. Enhanced synthesis of the 32-kDa protein was observed after cells were incubated with CdCl2 or diethylmaleate and protein was subjected to SDS-PAGE followed by fluorography. Concomitantly, in both cell preparations an increase in heme oxygenase activity was observed. Proteins from CdCl2- and diethylmaleate-treated cells were subjected to Western blotting and protein crossreacting with either rabbit antibody to rat liver heme oxygenase-1 (32,000 Mr) or rat testis heme oxygenase-2 (36,000 Mr) quantitated. The analysis indicated that the CdCl2 treatment increased the intensity of the HO-1 band 5.5-fold while the diethylmaleate treatment increased it three-fold relative to control. Neither treatment affected the intensity of HO-2 antibody binding. Incubation of cells with buthionine sulfoximine, under conditions which resulted in greater than or equal to 90% of the intracellular glutathione being depleted, enhanced synthesis of a 32-kDa protein when assayed by SDS-PAGE. This protein exhibited a Mr similar to the 32-kDa protein induced by either CdCl2 or diethylmaleate treatment. Proteins from buthionine sulfoximine and diethylmaleate-treated cells were mixed together and subjected to 2D PAGE. The resulting fluorograph demonstrated that both treatments produced identical patterns. In contrast, incubation of cells in diamide, a thiol oxidizing compound, resulted in enhanced synthesis of the 110-, 90-, and 73-kDa heat shock proteins but not the 32-kDa protein. The data presented have shown that depletion of glutathione by two independent methods, conjugation and inhibition of synthesis, enhances the synthesis of a 32-kDa protein identified as heme oxygenase-1; oxidation of glutathione, on the other hand did not. We interpret this to indicate that glutathione depletion rather than conjugation or oxidation represents one pathway for induction of heme oxygenase-1.
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20 MeSH Terms
Nitric oxide generation from nitroprusside by vascular tissue. Evidence that reduction of the nitroprusside anion and cyanide loss are required.
Bates JN, Baker MT, Guerra R, Harrison DG
(1991) Biochem Pharmacol 42 Suppl: S157-65
MeSH Terms: Animals, Cyanides, Endothelium, Vascular, Hemeproteins, Hydrogen-Ion Concentration, Luminescent Measurements, Male, Microsomes, Liver, Nitric Oxide, Nitroprusside, Oxidation-Reduction, Photochemistry, Rats, Rats, Inbred Strains, Temperature
Show Abstract · Added December 10, 2013
Nitric oxide (NO) was produced from sodium nitroprusside in the presence of vascular tissue but was not released spontaneously from the nitroprusside anion. In the absence of tissue in the dark nitroprusside did not release NO. When solutions of nitroprusside alone were irradiated with visible light, nitric oxide was released at rates linearly proportional to nitroprusside concentration and light intensity. Nitric oxide was produced from solutions of nitroprusside in the dark after the addition of vascular tissue, including lengths of rabbit aorta, subcellular fractions of aorta, and human plasma. NO was also released from nitroprusside after reaction with various reducing agents including cysteine and other thiols, ascorbic acid, sodium dithionite, ferrous chloride, hemoglobin, myoglobin, and partially purified cytochrome P450 with an NADPH-regenerating system. HCN was simultaneously produced in these solutions, and addition of KCN blocked NO release. Iodine oxidized intermediate cyanoferrates and blocked nitric oxide release. KCN or iodine also blocked NO production by tissue, but had no effect upon photochemical NO release. These results show that, apart from photolysis which makes no physiological contribution, release of nitric oxide from nitroprusside, in simple solutions and in biological tissue, occurs after nitroprusside has undergone reduction and lost cyanide.
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15 MeSH Terms