Abstract:
:Three phase partitioning is a process in which mixing t-butanol with ammonium sulphate with a protein solution leads to the formation of three phases. Generally, the interfacial protein precipitate (formed between upper t-butanol rich and lower aqueous phase) can be easily dissolved back in aqueous buffers. In case of ovalbumin, this led to a precipitate which was insoluble in aqueous buffers. This precipitate when solubilized with 8 M urea and subjected to three phase partitioning under various conditions led to many refolded soluble conformational variants of ovalbumin. One of these showed trypsin inhibitory activity, had marginally higher β-sheet content and had higher surface hydrophobicity (both with respect to native ovalbumin). Scanning electron microscopy and Atomic force microscopy of this preparation showed a thread like structure characteristic of amyloid fibrils. The behaviour of ovalbumin during three phase partitioning makes it a valuable system for gaining further understanding of protein aggregation.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Rather GM,Gupta MNdoi
10.1016/j.ijbiomac.2013.06.008subject
Has Abstractpub_date
2013-09-01 00:00:00pages
301-8eissn
0141-8130issn
1879-0003pii
S0141-8130(13)00336-Xjournal_volume
60pub_type
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