Abstract
Crystallins are a family of water-soluble proteins that constitute up to 90% of the water-soluble proteins in mammalian eye lenses. We present in this paper an alternative purification method for these proteins using polyethylene glycol/dextran aqueous two-phase extraction. Under the appropriate conditions, we were able to recover the γ-crystallin fraction essentially free of the remaining proteins. High concentrations of salt at a neutral pH maximize the recovery of γ-crystallins in the top phase and minimize the contamination by the other proteins present in the lenses. The proposed protocol decreases the separation time by about 50%. The complex partition behavior observed for these proteins reflects a delicate balance between protein/phase-forming species (various polymers and salts) and protein/protein interactions. This is evidenced, in part, by the role played by the largest proteins in this group as a "pseudo" phase-forming species.
Recommended Citation
O. Bermudez and D. Forciniti, "Purification and Characterization of Crystallins by Aqueous Two-phase Extraction," Biotechnology and Bioprocess Engineering, vol. 6, no. 6, pp. 395 - 401, Springer, Jan 2001.
The definitive version is available at https://doi.org/10.1007/BF02932320
Department(s)
Chemical and Biochemical Engineering
Keywords and Phrases
Aqueous two-phase systems; Crystallins; Purification
International Standard Serial Number (ISSN)
1226-8372
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2024 Springer, All rights reserved.
Publication Date
01 Jan 2001
