Abstract
Recombinant human ß-casein (CN) mutants were prepared having 11, 22 and 31 amino acids (aa) deleted from the C-terminus. The temperature-dependent self-association of these and the wild-type recombinant was studied by turbidity (OD400) while possible folding differences were examined by intrinsic and extrinsic fluorescence intensity and fluorescence resonance energy transfer. There were major self-association and some conformational differences. Hydrophobicity profile and hydrophobic cluster analysis for bovine and human ß-CN suggested that the ability of the 31 aa deletion mutant in human ß-CN to self-associate when a comparable bovine deletion peptide would not may be due to the presence of additional hydrophobic regions in the middle, indicating that the human protein may contain more than a single hydrophobic binding locus and suggesting that the process for the formation and structure of the micelles of human milk may be quite different from that for bovine milk. A new model may be needed.
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Abbreviations
- ANS:
-
8-anilino-1-naphthalene sulfonic acid
- CN:
-
casein
- FRET:
-
fluorescence resonance energy transfer
- WT, :
-
wild-type
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Bu, H., Sood, S.M. & Slattery, C.W. The Effect of C-Terminal Deletion on the Folding and Self-association of Recombinant Non-phosphorylated Human ß-Casein. Protein J 23, 509–517 (2004). https://doi.org/10.1007/s10930-004-7878-y
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DOI: https://doi.org/10.1007/s10930-004-7878-y