An investigation of “bound” water in frozen erythrocytes by proton magnetic resonance spin-lattice, spin-spin, and rotating frame spin-lattice relaxation time measurements

Zipp, Adam; Kuntz, Irwin D.; James, Thomas Leroy

doi:10.1016/0022-2364(76)90120-7

Cited by 14 publications

(11 citation statements)

References 34 publications

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“…The frequency dependence of T, and T1p observed here in barnacle muscle is similar to that found previously in other tissues (Held et al, 1973;Outhred and George, 1973;Knispel et al, 1974;Fung and McGaughy, 1974;Block and Maxwell, 1974;Finch and Homer, 1974;Civan and Shporer, 1975;Fung et al, 1975;Zipp et al, 1976). It leads to the inequality between T1 and T2, and can be due to several relaxation mechanisms.…”

Section: +±1supporting

confidence: 90%

“…5 and Table VI, and each of the correlation times used in our interpretation has been assigned a physical meaning. Several authors have argued for the presence of a complex distribution of exponential correlation functions, such as a single, continuous log-Gaussian distribution (Held et al, 1973, working with frog muscle) or two or more log-Gaussian distributions (Zipp et al, 1976, working with frozen erythrocytes) or a bimodal log power distribution (Outhred and George, 1973, working on toad muscle). In the absence of physical justiflcation for such distributions, however, our simpler model seems more appropriate.…”

Section: Finally Inmentioning

confidence: 99%

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Water in barnacle muscle. III. NMR studies of fresh fibers and membrane-damaged fibers equilibrated with selected solutes

Burnell¹,

Clark²,

Hinke³

et al. 1981

Biophysical Journal

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Water in barnacle muscle has been studied using NMR techniques. Fresh fibers are compared with membrane-damaged fibers treated with solutes that greatly alter fixed charge and total water content. Both water (97%) and solute (3%) protons are visible in continuous wave spectra of oriented fresh fibers. No local field inhomogeneities were detected, nor are cell solutes significantly bound. In pulse experiments, all cell water is visible and exhibits a single exponential decay. In fresh fibers, T2 approximately or equal to 40 ms; faster decaying signals are assigned to immobile and mobile protons on macromolecules. T1 and T1p are frequency dependent. Using equations derived for a two-compartment model with fast exchange, we calculate the following: tau b, the correlation time for anisotropic rotational motion of bound water; Sb, its order parameter; tau ex, the correlation time for exchange between bound and free fractions; f, the fraction of water bound; and Hr, the grams of water bound per gram of macromolecule. Whereas f varies inversely with total water content, the other parameters are virtually constant, with values: tau b approximately or equal to 1.3 X 10(-8) S; tau ex approximately or equal to 8 X 10(-6) s; Sb approximately or equal to 0.06; and Hr approximately or equal to 0.1g H2O/g macromolecule. Thus, the NMR relaxation detectable properties of water bound to macromolecules are unaffected by solutes that greatly alter the macromolecular surface charge.

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Section: +±1supporting

confidence: 90%

Section: Finally Inmentioning

confidence: 99%

Water in barnacle muscle. III. NMR studies of fresh fibers and membrane-damaged fibers equilibrated with selected solutes

Burnell¹,

Clark²,

Hinke³

et al. 1981

Biophysical Journal

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“…Just as the modified water structure near surfaces affects the short-range forces, so does it affect the dynamic properties-the viscosity, rheology, friction, 'lubricity,' various hydrodynamic interactions, 83,87 and also other important properties such as the diffusivity and melting point. Thus, the freezing points of liquids in narrow pores or thin films may be higher or lower (depending on whether the confining surface chemistry, lattice structure and pore geometry enhances or disrupts the liquid order) than the bulk values, 26,70 and molecular relaxation times can be orders of magnitude longer than in the bulk.…”

Section: Viscous and Lubrication Forces In Thin Aqueous Filmsmentioning

confidence: 99%

Static Forces, Structure and Flow Properties of Complex Fluids in Highly Confined Geometries

et al. 2005

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The Surface Forces Apparatus has been successfully used to measure the static and dynamic forces between surfaces across ultra-thin films of water and aqueous electrolyte solutions, and--more recently--polyelectrolyte-coated and articular cartilage surfaces in various solutions including hyaluronan, lubricin, and synovial fluid. The results give new insights into the lubricating action of biological lubricants such as synovial fluid and hyaluronan (a polysaccharide in synovial fluid), and biological surfaces such as phospholipid bilayers and cartilage surfaces. Contrary to earlier indications of long-range water-structuring at biological surfaces, more recent measurements clearly show that the viscosity of physiologically concentrated water (saline) is bulk-like beyond the first 1 or 2 layers from a single surface, and beyond 4-6 layers in thin films between two surfaces (the structure and forces may, however, be affected to larger distances). This implies that most structural, interaction force, and viscosity-related phenomena are determined--not only by the properties of the solvent (water)per se--but also by the surfaces and the water, ions, solutes, and macromolecules (proteins, polymers) exposed or adsorbed at the surfaces and, to a lesser degree, dissolved in the solvent. However, sometimes it is difficult to make a clear differentiation, e.g., one could consider hydration or surface-bound 'structured' water as part of the surface or as part of the intervening water between the two surfaces.

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“…iB) and proton (1) peaks. This organic fraction would be particularly important when nonfreezable water is studied at low temperature (7)(8)(9)(10) and when dehydrated muscle is investigated (11, 12). It has been shown that the deuteron signal does not have a millisecond fraction in the free induction decay (14) or spin echoes (4).…”

mentioning

confidence: 99%

Carbon-13 and proton magnetic resonance of mouse muscle

Fung¹

1977

Biophysical Journal

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It is shown that roughly 4 mmol carbon atoms/g mouse muscle can give rise to a "high resolution" 13C NMR spectrum. From the 13C spectrum, it is estimated that the protons from mobile organic molecules or molecular segments amount to 6-8%of total nonrigid protons (organic plus water) in muscle. Their spin-spin relaxation times (T2) are of the order of 0.4-2 ms. At 37 degrees C, the proton spin-echo decay of mouse muscle changes rapidly with time after death, while that of mouse brain does not.

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An investigation of “bound” water in frozen erythrocytes by proton magnetic resonance spin-lattice, spin-spin, and rotating frame spin-lattice relaxation time measurements

Cited by 14 publications

References 34 publications

Water in barnacle muscle. III. NMR studies of fresh fibers and membrane-damaged fibers equilibrated with selected solutes

Water in barnacle muscle. III. NMR studies of fresh fibers and membrane-damaged fibers equilibrated with selected solutes

Static Forces, Structure and Flow Properties of Complex Fluids in Highly Confined Geometries

Carbon-13 and proton magnetic resonance of mouse muscle

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