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Query: HUMANGGP:001372 (ESR)
 7,313 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The organization of lipids in sarcoplasmic reticulum membrane was studied with a variety of stearic spin labels and a phosphatidylcholine spin label. The ESR spectra of the spin-labeled membranes consisted of two components, one due to labels in lipid bilayer structure and the other due to more immobilized labels. The relative intensity of the immobilized component increased when the lipid content of the membrane was decreased by treatment with phospholipase A [EC 3.1.1.4] and subsequent washing with bovine serum albumin. Membrane containing 30% of the intact phospholipid, i.e.0.15 mg of phospholipid per mg of protein, showed a spectrum consisting only of the immobilized component (the overall splitting ranged from 58.5 G to 60.5 G). The immobilized component was ascribed to lipids complexed with protein. The fraction of lipids in the two different organizations was determined from the ESR spectrum. The activity of the Ca2+-Mg2+ dependent ATPase [ATP phosphohydrolase, EC 3.6.1.3] was found to increase almost linearly with the lipid bilayer content in the membrane, whereas phosphoenzyme formation was almost independent of the bilayer content. This indicated that the bilayer structure is necessary for the ATPase to attain its full transport activity.
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PMID:Organization of lipids in sarcoplasmic reticulum membrane and Ca2+-dependent ATPase activity. 17 48

1. 12-Nitroxide stearate binds to bovine serum albumin at about four independent and equivalent binding sites with an association constant of about 10(6) M-1. The binding at these high affinity binding sites is significantly reduced by addition of unlabeled stearate. These data suggest that nitroxide stearates probe the high affinity binding sites for long-chain fatty acids. 2. Qualitative analyses of the ESR spectra of 5-, 12- and 16-nitroxide stearate bound to bovine serum albumin and measurements of the interaction of these compounds so bound with ferricyanide ion provide a rough description of the binding site as follows: the polar headgroup of the spin-labeled fatty acid is rigidly fixed, but fairly accessible to paramagnetic ions. The middle part of the hydrocarbon chain of bound stearate spin label also is rigidly fixed but differs in being shielded from the solvent, presumably by a hydrophobic cleft. The methyl terminus shows greater motion, appearing to move within a narrow cone, and also appears to be somewhat accessible to paramagnetic ions.
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PMID:Binding of nitroxide stearate spin labels to bovine serum albumin. 18 32

The dependence from temperature and viscosity of the shifts of the internal and external wide extremums in the ESR spectra of spin labelled bovine serum albumin has been studied. 2,2,6,6-tetramethylpiperidine-NI-oxyl-4-iodacetamide was used as a spin label. The obtained dependences was shown to be a consequence of the label participation in two types of rotations: an anisotropic fast rotation with tau less than 10(-9) sec relatively to a macromolecule, and the isotropic one with tau greater than 10(-8) sec due to rotation of the macromolecule itself. These conclusions were done on the basis of a model for complex rotation of the spin label. Comparison of theoretical and experimental data makes it possible to determined the correlation time for the protein moiety, to evaluate quantitatively the polarity of surroundings of the iminoxyl and to introduce a numerical parameter for the degree of mobility of the spin label relatively to protein molecule.
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PMID:[Macromolecule rotative correlation time measurement by ESR for covalently bound spin label]. 22 33

The complex between bovine serum albumin (BSA) and benzo[a]pyrene (BaP) exhibits three different types of fluorescence. The visible fluorescence at 407, 431 and 458 nm is modified by the formation of both hydroxy-BaP derivatives and BaP products strongly bound to the protein. The ultraviolet fluorescence I is characterized by a triple-peaked structural fluorescence with maxima at 340, 357 and 378 nm. Upon addition of mercaptoethanol, this ultraviolet fluorescence decreases. The ultraviolet fluorescence II appears at 380 nm and corresponds to that of pyrene-like products. When irradiated with ultraviolet (365 nm) light, both the ultraviolet fluorescence I and the visible fluorescence decreases. In the interactionsof BaP with BSA, a new radical has also been found in addition to the known 6-oxo-BaP radical. The lyophilized BSA-BaP complex exhibits two broad ESR bands, one of which increases in lipid-free BSA. In the concentrated aqueous solution of the BSA-BaP complex, the ESR signal is converted to a six-line spectrum. The benzene extract, which removes non-covalently bound BaP products, shows an ESR signal similar to that in aqueous solution except for the absence of two lower g-valued lines. When irradiated with ultraviolet (365 nm) light the signal intensity of the new radical species decreases, while that of 6-oxo-BaP increases. Upon addition of of mercaptoethanol, the signal of the new radical also diminishes and is replaced by a single narrow signal. Ths mixture of BaP and cysteine kept at room temperature for one day in the dark produces both a six-line ESR spectrum and a broad ultraviolet fluorescence at 330 nm, which gradually decay in about one week. When BaP and cysteine are mixed at 65 degrees C for several hours, little ultraviolet fluorescence and ESR signal are detected. The results indicate the formation of a BaP radical as an intermediate in the interaction of BaP with BSA and cysteine in the presence of oxygen and suggest the involvement of SH-groups in this interaction.
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PMID:Benzo[a]pyrene--serum : albumin/cysteine interactions: fluorescence and electron spin resonance studies. 22 14

The microflora of the jejunum, ileum, and colon has been studied from operative samples in Crohn's disease (n = 30), ulcerative colitis (n = 15), and controls (n = 40). There was no significant difference in the flora of patients with ulcerative colitis compared with controls. In Crohn's disease there was a significant increase in E. coli (P less than 0.001) and B. fragilis (P less than 0.001) in the ileum and of E. coli (P less than 0.001) and lactobacilli (P less than 0.01) in the colon. The abnormal ileal flora in Crohn's disease was unrelated to serological evidence of disease activity (indices: ESR, serum albumin, serum seromucoids), diameter of the ileum, or excision of the ileocaecal valve. The abnormal colonic flora in Crohn's disease was not related to presence of macroscopic colitis.
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PMID:Influence of inflammatory bowel disease on intestinal microflora. 36 59

Conditions for the restoration of catalytic activity from heavy and light subunits which had been isolated from methylamine dehydrogenase of Pseudomonas sp. J were investigated in vitro. Maximal restoration of the activity was obtained in 0.8 M potassium phosphate buffer, pH 7.0-9.3, at 30 degrees C with equimolar concentrations of the two subunits. Under the optimal conditions, the recovery of enzyme activity was 86% and the time required for half-maximal recovery was about 3 min. Addition of bovine serum albumin or p-chloromercuribenzoate to the incubation mixture had no effect on the rate or extent of recovery of the enzyme activity. When the heavy subunit was added to the light subunit, the absorption spectrum of the light subunit changed to a form similar to that observed for the native enzyme. The concentration of methylamine required to change the spectrum of the light subunit was greatly decreased in the presence of the heavy subunit. Reconstituted enzyme was prepared from the isolated subunits and purified by gel chromatography. The reconstituted enzyme resembled the native enzyme in specific activity, molecular weight, substrate specificity, reaction mechanism, Michaelis constants for methylamine and phenazine methosulfate, susceptibility to inhibitor, and absorption, fluorescence and ESR spectra. However, it was less stable than the native enzyme to thermal and pH treatments. The CD spectrum was also slightly different from that of the native enzyme.
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PMID:Methylamine dehydrogenase of Pseudomonas sp. J. Reconstitution from its subunits. 67 Jan 54

Immune arthritis in sensitized rabbits was induced by intraarticular injection of bovine serum albumin. The development of the arthritis was accompanied by an increase in ESR, a rise of the level of serum CRP, caeruloplasmin and CIC. A chemiluminescent response of the whole blood phagocytes to stimulation by barium sulfate crystals, serum beta-glucuronidase and red cell superoxide dismutase activity enhanced, plasma malone dialdehyde content rose, serum SH groups diminished.
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PMID:[The effect of intra-articular emoxipin injections on the course of immune arthritis in rabbits]. 128

The formation of nonenzymatic glycosylation products appears to be a link between chronic hyperglycaemia and long-term diabetic complications. However, little is known concerning the glycation-induced modifications in the structure and conformation of proteins, which possibly underlie their altered functional characteristics. This study conveys a direct evidence for and compares the glucose-induced modifications in the conformation of three proteins with various half-lives: bovine serum albumin, human haemoglobin and bovine tendon collagen. These proteins incubated in vitro with glucose in various media containing optionally EDTA and Fe2+ ions contained up to 4-10 times as much attached glucose as did their relevant controls, and the extent of glycation was the highest in the samples incubated under air or in the absence of EDTA. The fluorescence and ESR data indicate that the Trp in albumin molecule, given albumin glycation-induced structural modifications, became more exposed to water surrounding solution whereas the Trp residues of haemoglobin remained shielded from water; also collagen fluorescence derived from the supposedly newly formed covalent crosslinks is vastly increased, and particularly when collagen was glycated under air or in the presence of Fe2+ ions. Possible mechanisms underlying the increased mobility of selected protein domains and glycation-mediated alterations in protein conformation are considered and discussed.
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PMID:Direct evidence for the alterations in protein structure and conformation upon in vitro nonenzymatic glycosylation. 132 46

The effects of bilirubin on the membrane motion parameters of human erythrocyte membrane were determined by the spin labelled ESR method. It causes a decrease in the order parameter and an increase in the corresponding fluidity of the lipid molecules. Bovine serum albumin was found to inhibit effectively the effects due to bilirubin. The disturbance to the organization of membrane molecules by bilirubin as well as the protective effects of serum albumin are discussed on the basis of the experimental results.
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PMID:The influence of bilirubin on fluidity and rotational correlation times of human erythrocyte membrane. 132 45

An ELISA was used to measure concentrations of soluble interleukin-2 receptor (sIL-2R) alpha chain in the sera of patients with Crohn's disease. In a group of 56 patients, serum concentrations of sIL-2R were significantly raised in patients with active disease compared with patients with inactive disease and age-matched control populations. There was a significant correlation between serum sIL-2R concentration and disease activity as assessed by the Harvey-Bradshaw index (r = +0.60; P less than 0.001) and laboratory measurements of disease activity including C-reactive protein (r = +0.79; P less than 0.001), ESR (r = +0.64; P less than 0.001) and platelet count (r = +0.533; P less than 0.001). We also found a negative correlation between sIL-2R levels and serum albumin (r = -0.66; P less than 0.001). In longitudinal studies, changes in the concentration of serum sIL-2R reflected the changes in disease activity. Soluble IL-2R, therefore, offers a new measure of disease activity in Crohn's disease with a potential advantage over other laboratory parameters currently available in that it may reflect more accurately the underlying immunopathogenic process.
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PMID:Soluble interleukin-2 receptor and disease activity in Crohn's disease. 162 35


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