Title : [Refolding of reduced/denatured RNase A the hydrophobic liquid-solid interface].

Pub. Date : 2010 Aug

PMID : 21261048






3 Functional Relationships(s)
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1 The results indicated that the reduced/ denatured RNase A can be refolded completely under the optimized conditions of pH 8.0, 2.0 mol/L urea and the concentration ratio of GSH/GSSG of 8: 1 in mobile phase. Urea ribonuclease A family member 1, pancreatic Homo sapiens
2 When the denatured protein was at the concentration of 5.0 mg/mL, the bioactivity efficiency and mass recoveries were 98.0% and 61.9% for 8.0 mol/L urea-denatured RNase A, respectively; and 100.1% and 66.8% for 7.0 mol/L guanidine hydrochloride (GuaHCl)-denatured RNase A, respectively. Urea ribonuclease A family member 1, pancreatic Homo sapiens
3 When the denatured protein was at the concentration of 5.0 mg/mL, the bioactivity efficiency and mass recoveries were 98.0% and 61.9% for 8.0 mol/L urea-denatured RNase A, respectively; and 100.1% and 66.8% for 7.0 mol/L guanidine hydrochloride (GuaHCl)-denatured RNase A, respectively. Urea ribonuclease A family member 1, pancreatic Homo sapiens