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D D Miller D L Johnston D Dragotakes J B Newell T Aretz H L Kantor T J Brady R D Okada 《Magnetic resonance imaging》1989,7(1):79-88
To determine how administration of a hyperosmotic agent alters regional nuclear magnetic resonance (NMR) relaxation parameters and imaging characteristics in ischemic-reperfused myocardium, 7 dogs were infused with mannitol for 15 minutes before and after the release of a 3 hour left anterior descending coronary artery (LAD) occlusion. Nine control animals received normal saline during the 3 hour occlusion and 1 hour reperfusion periods. Normal posterior left ventricular (LV) wall and the ischemic anterior LV wall (risk area) myocardium was sampled for calculation of segmental microsphere myocardial blood flow, % tissue water content, NMR relaxation times (T1, T2) and myocyte ultrastructure using electron microscopy. Mean infarct T1 values were 14% greater than normal segments in saline-treated controls, but only 5% greater after mannitol. The difference in tissue water content between infarcted and normal segments was 4% in saline-treated (83 vs. 79%) compared to 2% in mannitol-treated dogs (79 vs. 77%). T1, T2 and % water content of control infarct segments were greater than treated infarcts (p less than 0.01). T1 and T2 rose as occlusion flow fell below 0.5 ml/min/g in control hearts but did not rise until flows were reduced to 0.1 ml/min/g in mannitol-treated hearts. Areas of increased signal in T1 and T2 NMR images correlated well with histochemical infarct volume (r = 0.98, SEE = 1.1 cc) in mannitol-treated dogs, but infarct borders were qualitatively less well-defined than in controls. We concluded that mannitol (1) diminishes tissue edema and reduces NMR relaxation parameters (T1, T2) in infarcted myocardium; and (2) attenuates the rise in T1 and T2 and ultrastructural myocyte injury in ischemic-reperfused myocardium. 相似文献
134.
Preparation and water relaxation properties of proteins labeled with paramagnetic metal chelates 总被引:1,自引:0,他引:1
The proteins bovine serum albumin (BSA) and bovine immunoglobulin (IgG) have been labeled with paramagnetic gadolinium (III) and manganese (II) complexes using the bifunctional chelate approach. Diethylenetriaminepentaacetic acid (DTPA) and ethylenediaminetetraacetic acid (EDTA) were attached to several free amino groups on the proteins using cyclic anhydride forms of these ligands. The incorporation of the metal ions Gd+3 and Mn+2 into the chelating groups yielded highly paramagnetic proteins. The water relaxation ability (or relaxivity) of the protein-bound chelates at 20 MHz was found to be superior to that of the free metal complexes. Differences in relaxivity between the DTPA and EDTA conjugates could largely be accounted for by differences in the metal ion exposure to water. This labeling technique can be used in the preparation of intravascular NMR contrast agents (like paramagnetically-labeled human serum albumin) or target-specific agents (labeled monoclonal antibodies or fibrinogen). 相似文献
135.
Partlan MD Albergo S Bieser F Brady FP Caccia Z Cebra D Chacon AD Chance J Choi Y Costa S Elliott JB Gilkes ML Hauger JA Hirsch AS Hjort EL Insolia A Justice M Keane D Kintner J Lisa MA Matis HS McMahan M McParland C Olson DL Peilert G Porile NT Potenza R Rai G Rasmussen J Ritter HG Romanski J Romero JL Russo GV Scharenberg RP Scott A Shao Y Srivastava BK Symons TJ Tincknell ML Tuvé C Wang S Warren PG Wieman HH Wolf K 《Physical review letters》1995,75(11):2100-2103
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The reaction of diphenyl-, dichloro-, and chloroketenes with several siloxy dienes results in (4 + 2) and/or (2 + 2) cycloaddition products depending primarily on Substitution in the diene. The (4 + 2) cycloaddition products are easily hydrolyzed to pyranones. These results are discussed in terms of a dipolar intermediate. 相似文献
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Mason PE Dempsey CE Neilson GW Brady JW 《The journal of physical chemistry. B》2005,109(50):24185-24196
Neutron diffraction experiments and molecular dynamics simulations are used to study the structure of aqueous solutions of two electrolytes: guanidinium sulfate (a mild protein conformation stabilizer) and guanidinium thiocyanate (a powerful denaturant). The MD simulations find the unexpected result that in the Gdm2SO4 solution the ions aggregated into mesoscopic (nanometer-scale) clusters, while no such aggregation is found in the GdmSCN solution. The neutron diffraction studies, the most direct experimental probe of solution structure, provide corroborating evidence that the predicted very strong ion pairing does occur in solutions of 1.5 m Gdm2SO4 but not in 3 m solutions of GdmSCN. A mechanism is proposed as to how this mesoscopic solution structure affects solution denaturant properties and suggests an explanation for the Hofmeister ordering of these solutions in terms of this ion pairing and the ability of sulfate to reverse the denaturant power of guanidinium. 相似文献