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Many of the integral membrane proteins of E. coli have been solubilized successfully with detergents and organic solvents.
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Detergents are commonly used to solubilize membrane proteins, and many membrane proteins have been solubilized with various detergents without the loss of biological activity [25].
The recombinant pro-ervatamin-C was expressed as inclusion body using pET-28a vector and the protease was solubilized, purified and successfully refolded to its functionally active form.
After decalcification, the cells were washed three times with PBS and the cells were solubilized with 0.1 N NaOH/0.1% SDS.
Hemicellulose and lignin are solubilized with minimal degradation, and the hemicellulose is converted to sugars with acid pretreatment.
After the washing with phosphate-buffered saline, the stained cells were solubilized with 70% ethanol.
SRB was solubilized with 100 μl of 10 mM Tris buffer for 5 min with shaking.
Subsequently, the solution was aspirated and the insoluble formazan product was solubilized with acidified iso-propanol.
After incubation for 4 h, the formazan crystals were solubilized with 150 μL of DMSO.
The plates were air dried; the bound dye was solubilized with 200 μL of 33% (v/v) glacial acetic acid.
The dye incorporated by the adherent cells was solubilized with 200 μl of 95% (v/v) ethanol.
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