Department of Ophthalmology, Jawaharlal Nehru Medical College and Hospital, Rajasthan, India
Research Article
Differential Proteolytic Stabilities of Soluble Proteins and Amyloid Like Protein Aggregates Isolated from Human Cataract Eye Lenses
Author(s): Chandrika Mittal, Ram Swaroop Harsolia and Jay Kant Yadav*
Background: The cross β-sheet structures in amyloids are usually proteolytic resistant. The amyloid like protein aggregates derived from human cataracts are distinct in the sense that they do not exist as fibrils rather they are found to be aggregates of sequestered crystalline.
Methods: The proteolytic susceptibility was measured by recording changes in the Congo Red (CR) bathochromic shifts, Thioflavin T (ThT) and 8-Anilino-1-Naphthalene Sulfonic acid (ANS) fluorescence emission. The difference between the degradation patterns of these two fractions of the isolated protein was further estimated by Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE). Furthermore, to substantiate the data regarding the proteolytic degradation of aggregated crystalline, the native PAGE has been performed which provided an evident confirm.. View More»