Skip to main content

Table 1 Batchwise refolding of denatured and reduced RNase A and CHMO.

From: Folding machineries displayed on a cation-exchanger for the concerted refolding of cysteine- or proline-rich proteins

   RNase A CHMO
Refolding condition Refolding yield* (%) Activity yield (%) Refolding yield (%) Activity yield (%)
SP Sepharose Fast Flow alone (control) 17.2 ± 1.4 33 ± 3 2.1 ± 0.7 17 ± 2
Single refolding matrix Mini-chaperone 55.0 ± 2.1 98 ± 5 31.0 ± 1.6 107 ± 6
  DsbA 57.6 ± 2.4 121 ± 12 8.5 ± 1.3 99 ± 3
  hPPIase 67.0 ± 3.3 115 ± 9 11.0 ± 2.2 103 ± 8
Binary refolding matrix Mini-chaperone + DsbA 68.0 ± 1.8 107 ± 5 27.1 ± 2.4 109 ± 11
  Mini-chaperone + hPPIase 56.7 ± 2.7 118 ± 7 46.2 ± 1.8 123 ± 8
  DsbA + hPPIase 58.4 ± 2.6 126 ± 2 13.8 ± 1.5 111 ± 10
Ternary refolding matrix Mini-chaperone + DsbA + hPPIase 73.0 ± 1.5 131 ± 3 53.0 ± 2.7 125 ± 4
  1. Data were collected from three independent refolding experiments with identical protein concentration.
  2. * Refolding yield: the ratio of the soluble protein to the total amount of denatured and reduced protein used for refolding.
  3. Activity yield: the specific activity of the recovered soluble protein relative to that of native RNase A or CHMO showing 76% or 80% of the specific activity of the purest protein obtained from Sigma Company