Publications by authors named "Frederick A Bettelheim"

Purpose: Syneretic response to pressure variation of 1 atm or more has been demonstrated previously in bovine and human lenses with nuclear magnetic resonance (NMR) relaxation measurements. This study is designed to prove that a similar response is observable in smaller pressure increments closer to the normal physiological range.

Methods: Excised calf eyes were enucleated, the lenses dissected out, and immersed in medium.

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This paper briefly reviews light scattering methodologies in lens research. In the phenomenological sense cataract formation (lens opacities or turbidities) in its early stages can be described by enhanced scattering of light. In the analytical sense information is obtained on the molecular entities involved in light scattering.

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The distribution of particle sizes was studied in six regions of human liquid vitreous samples. Particle sizes were calculated from dynamic light scattering measurements as hydrodynamic diameter of molecules. In general, particle sizes increased progressively from anterior (near lens) to posterior (near retina).

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Purpose: The study was designed to observe whether a reversible syneretic response to pressure is operative in normal human lenses and whether such a response demonstrates a uniform age dependence.

Methods: Seven sections (from the anterior outer cortex to the posterior outer cortex) of 10 human lenses were imaged at 2 atmospheres (atm) pressure and the T(1) (spin-lattice) and T(2) (spin-spin) relaxation data on each section were collected. The pressure was then released and NMR relaxographic data were collected under 1 atm.

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Ten excised normal human lenses of various ages were studied. Seven sections of each lens, from anterior outer cortex to posterior outer cortex were imaged and the T(1) (spin-lattice) and T(2) (spin-spin) relaxation data on each section were collected. T(1) and T(2) relaxation were analysed by fitting pixel intensity to one term exponential expressions.

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Molecular chaperones prevent the aggregation of partially folded or misfolded forms of protein. alpha-Crystallin performs such a function in the ocular lens. Dynamic light scattering (DLS) measurements were performed to gain insight into the kinetics and mechanism of alpha-crystallin chaperoning.

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