Dynamics of fluid/particulate mixtures in tube flow.

Magnetic resonance imaging (MRI) techniques have been utilized to experimentally measure the velocity profile of fluid/particulate mixtures as a function of flow rate, particle loading, and particle size. The experimental velocity profiles in tube flow were described by a power law model; the power law parameter decreased as flow rate, particle loading, and particle size increase. This work is relevant to aseptic processing of particulate foods.

Nuclear magnetic resonance as a measure of cerebral metabolism: effects of hypertonic saline resuscitation.

UNLABELLED: Fears of central nervous system dysfunction from acute hypernatremia and hyperosmolarity with hypertonic saline resuscitation are often cited. We used high-energy phosphate nuclear magnetic resonance to investigate resuscitation effects on cerebral metabolism. Rats were instrumented for hemodynamic monitoring and fluid infusion and a phosphorus surface coil placed on their skulls. After shimming, baseline spectra were obtained. Animals were then bled for one hour to a mean arterial pressure (MAP) of 45 mm Hg, followed by resuscitation for one hour to a MAP of 75 mm Hg with lactated Ringer's (LR, n = 17) or 7.5% hypertonic saline (HS, n = 25). Spectra were obtained again and analyzed for the ratio of high-energy phosphocreatine (PCr) to low-energy inorganic phosphate (Pi). Intracellular hydrogen ion concentration [H+] was calculated from the PCr/Pi shift. [table: see text] CONCLUSIONS: (1) Hypertonic saline results in a decreased intracellular pH compared with LR without associated changes in high-energy phosphate metabolism. (2) Decreases in pH may be the result of cell dehydration rather than metabolic dysfunction.

Nuclear magnetic resonance as a noninvasive method of diagnosing intestinal ischemia: technique and preliminary results.

Despite the long-standing effort to identify a noninvasive method of diagnosing intestinal ischemia, no reliable biochemical or radiographic technique has evolved. We explored the use of phosphorus nuclear magnetic resonance (PNMR) as a method of detecting surgically induced intestinal ischemia. Using Lewis strain rats (250 to 300 g), small intestine ischemia was produced by ligation in succession from the ligament of Treitz to the ileocecal valve 1 of 2 (group I), 2 of 3 (group II), 3 of 4 (group III), and 4 of 5 (group IV) mesenteric terminal vessels. A sham-operated group was used as a control. Following the surgical procedure, the abdomen was closed and the rat positioned under the PNMR apparatus. Using phosphorus spectroscopy, data were analyzed using a computer program and plotted on a graph indicating relative peaks for the phosphate-based compounds. As a means of comparing groups, we devised an inorganic phosphate to phosphocreatine ratio ("ischemia index"), a qualitative measurement indicating trends used to evaluate ischemia. At the completion of the PNMR study, the abdomen was reopened and proximal, mid, and distal small intestine segments were harvested for histological evaluation using a previously established grading system for intestinal ischemia. Preoperatively, immediately postoperatively, and approximately 2 hours postoperatively, blood samples were obtained for hexosaminidase levels. With increasing vascular ligation, there was an upward trend in both the histological appearance of ischemia and the PNMR ischemia index indicative of increasing tissue ischemia. A similar trend was identified when the histological ischemia grade was directly correlated with the PNMR ischemia index. Hexosaminidase levels did not correlate with ischemia in this study.(ABSTRACT TRUNCATED AT 250 WORDS)

1H-NMR heme resonance assignments by selective deuteration in low-spin complexes of ferric hemoglobin A.

The heme methyl and vinyl alpha-proton signals have been assigned in low-spin ferric cyanide and azide ligated derivatives of the intact tetramer of hemoglobin A, as well as the isolated chains, by reconstituting the proteins with selectively deuterated hemins. For the hemoglobin cyanide tetramer, assignment to individual subunits was effected by forming hybrid hemoglobins possessing isotope-labeled hemins in only one type of subunit. The heme methyl contact shift pattern has 1-methyl and 5-methyl shifts furthest downfield in both chains and the individual subunits of the intact hemoglobin in both the cyanide- and azide-ligated species, which is consistent with a dominant rhombic perturbation due to the proximal His-F8 imidazole pi bonding in the known structure for human adult hemoglobin. The individual chain and subunit assignments confirm that the detailed electronic/magnetic properties of the heme pocket are essentially unaltered upon assembling the R-state tetramer from the isolated subunits.

Proton NMR characterization of isomeric sulfmyoglobins: preparation, interconversion, reactivity patterns, and structural features.

The preparations of sulfmyoglobin (sulf-Mb) by standard procedures have been found heterogeneous by 1H NMR spectroscopy. Presented here are the results of a comprehensive study of the factors that influence the selection among the three dominant isomeric forms of sperm whale sulf-Mb and their resulting detailed optical and 1H NMR properties as related to their detectability and structural properties of the heme pocket. A single isomer is formed initially in the deoxy state; further treatment in any desired oxidation/ligation state can yield two other major isomers. Acid catalysis and chromatography facilitate formation of a second isomer, particularly in the high-spin state. At neutral pH, a third isomer is formed by a first-order process. The processes that alter oxidation/ligation state are found to be reversible and are judged to affect only the metal center, but the three isomeric sulf-Mbs are found to exhibit significantly different ligand affinity and chemical stability. The present results allow, for the first time, a rational approach for preparing a given isomeric sulf-Mb in an optimally pure state for subsequent characterization by other techniques. While optical spectroscopy can distinguish the alkaline forms, only 1H NMR clearly distinguishes all three ferric isomers. The ring current shifts in the carbonyl complexes of reduced sulf-Mb complexes support saturation for a pyrrole in each isomer. The hyperfine shift patterns in the various oxidation/spin states of sulf-Mbs indicate relatively small structural alteration, and the proximal and distal sides of the heme suggest that peripheral electronic effects are responsible for the differentially reduced ligand affinities for the three isomeric sulf-Mbs. The first 1H NMR spectra of sulfhemoglobins are presented, which indicate a structure similar to that of the initially formed sulf-Mb isomer but also suggest the presence of a similar molecular heterogeneity as found for sulf-Mb, albeit to a smaller extent.