Regini, Justyn Wiktor ![]() ![]() |
Abstract
Purpose: The purpose of this study is to compare the structural integrity of bovine lenses using small-angle X-ray diffraction techniques, before and after freezing, using both liquid nitrogen and a −20°C freezer to understand the molecular changes that occur and to see if any permanent structural changes result from the freezing and thawing process. Materials and Methods: We used small-angle X-ray scattering to investigate the effects of freezing whole bovine eye lenses (i) in liquid nitrogen and (ii) at −20°C, to better understand the structural basis of the phase transitions. Results: Lenses frozen in liquid nitrogen thawed more rapidly than those placed at −20°C. With both freezing methods, X-ray patterns taken during the thawing process indicated less protein order than before or after freezing. After both freezing methods, the X-ray reflection returned to its original spacing and close to its original intensity values before freezing. Conclusions: We explain these phenomena in terms of a simple model based on the melting of ice crystals. We also suggest that the liquid nitrogen method of freezing is probably the better method of cryo-preservation for maintaining lens crystallin order.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Optometry and Vision Sciences |
Subjects: | R Medicine > RE Ophthalmology |
Additional Information: | crystallin proteins, freezing and short-range order, ice crystals, lens, X-ray |
Publisher: | Taylor and Francis |
ISSN: | 0271-3683 |
Last Modified: | 19 Oct 2022 09:57 |
URI: | https://orca.cardiff.ac.uk/id/eprint/22751 |
Citation Data
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