Abstract:
:Studies have followed the turbidity (OD400 nm) of beta-casein (CN) as temperature (T) increased from 4 to 37 degrees C. Native non-phosphorylated beta-CN showed a turbidity increase above 25 degrees C and precipitated at about 22 degrees C in 5mM Ca+2. These patterns were reproducible upon T-cycling while those of recombinant beta-CN proteins are not. Here, a wild-type recombinant that was thermally stable after being frozen in solution and stored at -20 degrees C for a prolonged period of time was denatured with guanidine HCl and refolded by dialysis against buffer. This protein was again not stable to T-cycling. A recombinant mutant with four extra N-terminal amino acids was very stable to T-cycling, both with and without 5mM Ca+2. However, it was still much different than the native protein. These results indicate that there are probably many energy minima for this protein and emphasize the possibility of "chaperon-like" conditions for proper folding of human beta-CN.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Sood SM,Booth C,Jhawar H,Slattery CWdoi
10.1016/j.abb.2006.07.008subject
Has Abstractpub_date
2006-10-01 00:00:00pages
55-8issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(06)00262-1journal_volume
454pub_type
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