α-lactalbumin: Of Camels and Cows
Document Type
Article
Publication Date
2016
Keywords
CD, Aggregation, Fluorescence, Guanidine Hydrochloride-mediated Unfolding, Intrinsically Disordered Protein, α-lactalbumin
Abstract
Since camel milk has been attributed with various medicinal properties not found in bovine milk, we are systematically examining the differences between different proteins in bovine and camel milk. The purpose of this study is to investigate the structural differences between the bovine and camel α- lactalbumins. α-Lactalbumin is a highly abundant protein present in the milk of all mammalian species. Here we found several structural differences between bovine and camel α-lactalbumins: camel protein is more stable towards thermal and pHmediated denaturation but less stable towards guanidine hydrochloride-mediated unfolding, aggregates faster and is predicted to be more disordered than bovine α- lactalbumin.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
Protein & Peptide Letters, v. 23, issue 12, p. 1072-1080
Scholar Commons Citation
Redington, Jeniffer M.; Breydo, Leonid; Almehdar, Hussein A.; Redwan, Elrashdy M.; and Uversky, Vladimir N., "α-lactalbumin: Of Camels and Cows" (2016). Molecular Medicine Faculty Publications. 866.
https://digitalcommons.usf.edu/mme_facpub/866
