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Presentation Presentation
Casein β -C-C- -C-C- C C 23983 Da Plasmin Plasmin P PPP P 1 15 17 17-19 19 35 105/106 209 28/29 107/108 Hydrophilic/charged - Amphiphilic Little charged Hydrophobe The France-Egypt Year Of Science And Technology, 2010
Chhaperone-like activity ac (%) Chaperone-like activities of native and mutant monomeric ββ-CN. CN TTarget t protein t i - iinsulin li 120 100 80 60 40 20 0 0 0,025 0,05 0,075 0,1 0,125 (ß-CN /Insulin) molar ratio Native β-CN (■), Wild type β-CN (□), C4 β-CN (▲) and C208 β-CN (∆) The France-Egypt Year Of Science And Technology, 2010 Chemically-induced aggregation of insulin performed f di in the th présence é of f 20 mM DTT at 40 °C. Mutant β-CNs exhibit considerably smaller chaperone chaperone-activities activities than that of native β-CN.
- Page 1 and 2: ENGINEERING OF DAIRY PROTEINS AND T
- Page 3 and 4: Average composition of f cow milk i
- Page 5 and 6: Caséine κ 169 aa 19037 Da 1 Chymo
- Page 7 and 8: P P P P β casein MKVLILACLV ALALAR
- Page 9 and 10: F I Trp 143 monomer λ ↑ °CC Int
- Page 11 and 12: Same conditions as for DLS. λmmax
- Page 13 and 14: SDS-PAGE of bovine β casein and mu
- Page 15 and 16: SDS-PAGE of the dimerizing β casei
- Page 17: Hydrophilic Hydrophilic-Hydrophilic
- Page 21 and 22: Consequence of Cys incorporation on
- Page 23 and 24: − Average IgE (ng/ml) 35 30 25 20
- Page 25: Our INRA team Isabelle Bronnec Aynu
Casein β<br />
-C-C-<br />
-C-C- C C<br />
23983 Da<br />
Plasmin Plasmin<br />
P PPP<br />
P<br />
1 15 17 17-19 19 35<br />
105/106<br />
209<br />
28/29 107/108<br />
Hydrophilic/charged -<br />
Amphiphilic<br />
Little charged<br />
Hydrophobe<br />
The France-Egypt Year Of Science And Technology, 2010
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