New insights into structural changes of lens proteins

Regini, Justyn Wiktor ORCID: https://orcid.org/0000-0001-6149-5893 2003. New insights into structural changes of lens proteins. Journal of Mechanics in Medicine and Biology 03 (01) , pp. 71-78. 10.1142/S0219519403000624

Full text not available from this repository.

Abstract

X-ray scattering techniques were used to study the effects of heating on whole eye lens and α-crystallin gels. The temperature range used was from 20 to 70°C. The position of single X-ray reflection seen in whole lens was unchanged in the temperature range 20 to 45°C, with a continuous spacing of 152 Å. However, at 50°C the spacing increased from 152 Å to 165 Å. An interpretation of these results is that in eye lens, α-crystallin is protecting other lens proteins from super-aggregation up to 50°C. In α-crystallin gels a moderate increase in both the spacing and intensity of the reflection was observed from 20 to 45°C, followed by a dramatic increase from 45 to 70°C. Over the whole temperature range the spacing changed from 138 Å at 70°C to 195 Å at 70°. After eleven hours of cooling, this effect was found to be irreversible.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Optometry and Vision Sciences
Subjects:	R Medicine > RE Ophthalmology
Uncontrolled Keywords:	Eye lens; α-crystallin; temperature; X-ray scattering
Publisher:	World Scientific Publishing
ISSN:	0219-5194
Last Modified:	24 Oct 2022 10:19
URI:	https://orca.cardiff.ac.uk/id/eprint/43845

Actions (repository staff only)

Edit Item