Refolding Record:
Protein | |
---|---|
Protein Name | Hen egg- white lysozyme |
Abbreviated Name | HEWL |
SCOP Family | C-type Lysozyme |
Structure Notes | |
Organism | Chicken (Gallus gallus) |
UniProt Accession | P00698 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Alpha+Beta |
Molecularity | Unknown |
Construct | |
---|---|
Full Length | y |
Domain | n/a |
Chimera | n/a |
Variants | n/a |
Chain Length | 126 |
Molecular Weight | 14471.1 |
Pi | 10.5 |
Molecular Weight | 14471.1 |
Disulphides | 4 |
Full Sequence |
MKSAVLFLLGIIFLEQCGVRGTLVIRNARCSCISTSRGTIHYKSLKDLKQFAPSPNCNKTEIIATLKNGDQTCLDPDSANVKKLMKEWEKKINQKKKQKRGKKHQKNMKNRKPKTPQSRRRSRKTT
|
Notes | n/a |
Expression | |
---|---|
Report | Mannall GJ, Titchener-Hooker NJ, Dalby PA (2007) Biotechnology and Bioengineering, 97, 1523-1534 |
Project Aim | Protein refolding |
Fusion | None |
Protein Expression and Production | Protein expressed and purified in native conformation prior to denaturation and refolding. |
Expression Host | None |
Expression Strain | None |
Expression Temp | 0.0 |
Expression Time | 0 |
Expression Vector | |
Expression Protocol | |
Method of Induction | Not Stated |
Cell Density at Induction | OD = |
Cell Disruption Method | None |
Lytic Agent | None |
Pre-Refolding Purification | RP-HPLC |
Solubility |
Refolding | |
---|---|
Refolding Method | Dilution |
Wash Buffer | 8 M GdHCl, 32 mM DTT, 50 mM Tris, 1 mM EDTA pH 8 |
Solubilization Buffer | 5o mM Tris HCl, 4 mM Cytamine, 1 mM EDTA, (0,0.167,0.47,0.717,0.967,1.967) mM GdHCl pH 7 |
Refolding Buffer | 5o mM Tris HCl, 4 mM Cytamine, 1 mM EDTA, (0,0.167,0.47,0.717,0.967,1.967) mM GdHCl pH 7 |
Pre-Refolding Purification | RP-HPLC |
Tag Cleaved | no tag |
Refolding pH | 7.0 |
Refolding Temperature | 25.0 |
Protein Concentration | n/a |
Refolding Time | 2 h |
Redox Agent | Cystamine |
Redox Agent Concentration | 4 mM |
Refolding Protocol | Denatured reduced lysozyme (16 mg mL􏰁1) was diluted 1:15 in various refold buffers (six refold buffers in total as detailed in Table I) at ambient temperature and mixed vigorously for 30 s, and left at ambient temperature. After 2 h, a sample (2 mL) was taken and quenched with 10% v/v TFA (200 umL). A further sample was taken at 24 h and left unquenched. Samples were assayed for native lysozyme using RP-HPLC. |
Refolding Assay | Enzyme activity |
Refolding Chaperones | None |
Refolding Additives | None |
Additives Concentration | n/a |
Refolding Yield | n/a |
Purity | n/a |
Notes | n/a |