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
Back to article page

BMC Biotechnology

ISSN: 1472-6750

Contact us