A. Water Exchange 2326 B. Proton Exchange 2327 C. Electronic Relaxation 2327 D. Relaxivity 2331 E. Outerand Second-Sphere Relaxivity 2334 F. Methods of Improving Relaxivity 2336 V. Macromolecular Conjugates 2336 A. Introduction 2336 B. General Conjugation Methods 2336 C. Synthetic Linear Polymers 2336 D. Synthetic Dendrimer-Based Agents 2338 E. Naturally Occurring Polymers (Proteins, Polysaccharides, and Nucleic Acids) 2339

https://mriquestions.com/uploads/3/4/5/7/34572113/lauffer_1999_review.pdf

Gadolinium(III) Chelates as MRI Contrast Agents: Structure, Dynamics, and Applications

Publisher Summary Lectins play an important role in the development of immunology. Lectins also find application in serological laboratories for typing blood and determining secretor status, separating leucocytes from erythrocytes, and agglutinating cells from blood in the preparation of plasma. They serve as reagents for the detection, isolation, and characterization of carbohydrate-containing macromolecules, including blood-group antigens. In their interaction with saccharides, lectins serve as models for carbohydrate-specific antibodies, with the important advantage to purify lectins in gram quantities. Lectins are classified according to their carbohydrate-binding specificity that includes D-mannose(D-glucose)-binding lectins and 2-acetamido-2-deoxy-D-glucose-binding lectins. The chapter considers only those lectins that have been purified to homogeneity, and studied with regard to their biophysical, biochemical, and carbohydrate-binding specificity. The chapter also describes the cell-binding and biological properties of lectins. The chapter concludes with the description of several glycopeptide structures showing the carbohydrate-binding loci with which various lectins interact.

The lectins : carbohydrate-binding proteins of plants and animals

Knowledge of regional hemodynamics has widespread application for both physiological research and clinical assessment. Here we review the use of MR contrast agents to measure tissue perfusion. Two primary mechanisms of image contrast are discussed: relaxivity and susceptibility effects. Relaxivity effects result from dipolar enhancement of T1 and T2 rates. Because tissue T1 rates are intrinsically smaller, the dominant effect is shortening of T1 relaxation times. The second mechanism of image contrast is the variation in tissue magnetic field produced by heterogeneous distribution of high magnetic susceptibility agents. Quantitation of tissue perfusion requires a detailed understanding of the relation between contrast agent concentration and associated MR signal changes. Studies to date show a linear relationship between contrast agent concentration and rate change in most organs. The exact nature of this relationship in the dynamic setting of rapid contrast agent passage through the microcirculatory bed is less well established. If this relationship is known, tracer kinetic modeling can be used to calculate regional blood flow and blood volume. Data are presented which indicate that this approach is feasible, and suggest the potential of contrast-enhanced NMR for high resolution in vivo mapping of both physiology and anatomy.

Perfusion imaging with NMR contrast agents

Here we describe a glycan microarray constructed by using standard robotic microarray printing technology to couple amine functionalized glycans to an amino-reactive glass slide. The array comprises 200 synthetic and natural glycan sequences representing major glycan structures of glycoproteins and glycolipids. The array has remarkable utility for profiling the specificity of a diverse range of glycan binding proteins, including C-type lectins, siglecs, galectins, anticarbohydrate antibodies, lectins from plants and microbes, and intact viruses.

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Printed covalent glycan array for ligand profiling of diverse glycan binding proteins

The essential involvement of manganese in photosynthetic water oxidation was implicit in the observation by Pirson in 1937 that plants and algae deprived of Mn in their growth medium lost the ability to evolve O{sub 2}. Addition of this essential element to the growth medium resulted in the restoration of water oxidation within 30 min. There is increased interest in the study of Mn in biological chemistry and dioxygen metabolism in the last two decades with the discovery of several Mn redox enzymes. The list of enzymes where Mn is required for redox activity includes a Mn superoxide dismutase, a binuclear Mn-containing catalase, a binuclear Mn-containing ribonucleotide reductase, a proposed binuclear Mn site in thiosulfate oxidase, a Mn peroxidase that is capable of oxidative degradation of lignin, and perhaps the most complex and important, the tetranuclear Mn-containing oxygen-evolving complex in photosystem II (Mn-OEC). Mn is well suited for the redox role with accessible oxidation states of II, III, and IV, and possibly V: oxidation states that have all been proposed to explain the mechanisms of the Mn redox enzymes.

Manganese Cluster in Photosynthesis: Where Plants Oxidize Water to Dioxygen

Field-cycling relaxometry of protein solutions and tissue: Implications for MRI

Conformation states of concanavalin A: Kinetics of transitions induced by interaction with Mn2+ and Ca2+

Paramagnetic ions have been used to alter the magnetic relaxation rates 1/T1 and 1/T2 of solvent water protons since the first observations of a proton resonance signal almost four decades ago. The earliest theories of relaxation indicated that the influence of solute paramagnetic ions on relaxation rates of solvent protons should depend both on the chemical environment of the solute ions and on the magnetic field strength. Much knowledge, both experimental and theoretical, has since been amassed regarding relaxation effects in solutions of hydrated ions (aquoions) and of complexes of these ions with macromolecules, mainly proteins. The phenomena are well understood at this point, though the understanding is more retrospective than predictive for ion-protein complexes. Nonetheless, from what is now known about homogeneous solutions, and from current reports on the introduction of paramagnetic ions into tissue to alter contrast in NMR images by affecting relaxation rates, it is clear that the solution results are particularly germane, and transferable, to tissue investigations. The main features of relaxation of solvent protons in the presence of solute paramagnetic ions, as hydrated aquoions and complexed with protein, are presented here, with attention to those ions most relevant to in vivo studies, and with emphasis on the influence of the magnetic field and the chemical environment of these ions on solvent proton relaxation rates.

Relaxation of solvent protons by paramagnetic ions and its dependence on magnetic field and chemical environment: implications for NMR imaging.

Nuclear magnetic relaxation dispersion in protein solutions: V. Bovine erythrocyte superoxide dismutase

The magnetic field dependence of the longitudinal relaxation rates 1/T1 (NMRD profiles) of blood and plasma from rabbits before and after injection of Gd(DTPA) are reported as a function of magnetic field strength from 0.01 to 50 MHz. Over 100 values along the time-dependent magnetization were recorded for each 1/T1 and analyzed for multiple exponentials. From these data, which indicate a single exponential, from the measured Gd content of each sample, and the NMRD profiles, we show that Gd is in the extracellular space only and is present as rotationally mobile Gd(DTPA), uncomplexed with protein or blood cells; and that the water protons exchange rapidly between the intra- and extracellular regions.

Rodney D. Brown

Papers

Field-cycling relaxometry of protein solutions and tissue: Implications for MRI

Conformation states of concanavalin A: Kinetics of transitions induced by interaction with Mn2+ and Ca2+

Relaxation of solvent protons by paramagnetic ions and its dependence on magnetic field and chemical environment: implications for NMR imaging.

Nuclear magnetic relaxation dispersion in protein solutions: V. Bovine erythrocyte superoxide dismutase

Relaxation of water protons in the intra- and extracellular regions of blood containing Gd(DTPA).