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Table 1 Percentage of turbiditya of the DTT-denatured substrates

From: Investigation of the chaperone function of the small heat shock protein — AgsA

 

lysozyme

insulin

 

25°C

50°C

25°C

50°C

 

10 μM

20 μM

20 μM

10 μM

20 μM

20 μM

AgsA

12.3 ± 0.7

2.6 ± 0.2

2.9 ± 0.4

123.0 ± 0.4

119.7 ± 4.7

4.6 ± 0.3

ΔN11

8.8 ± 0.07

1.5 ± 0.2

1.1 ± 0.2

149.2 ± 7.4

132.8 ± 5.9

1.1 ± 0.3

ΔN17

10.0 ± 0.3

1.7 ± 0.2

5.0 ± 0.6

119.4 ± 0.6

11.1 ± 0.4

0.5 ± 0.3

ΔC11

114.2 ± 3.2

12.9 ± 0.4

231.1 ± 1.4

51.1 ± 1.3

1.5 ± 0.2

0.8 ± 0.08

  1. aThe percentage of turbidity showed the ratio of the turbidity of the DTT-denatured lysozyme (10 μM) or insulin (70 μM) with the indicated concentration of AgsA or its mutants to the turbidity of the DTT-denatured lysozyme or insulin alone (for details, see the Materials and Methods section). Values are the mean ± SD obtained from 3 independent experiments.
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BMC Biochemistry

ISSN: 1471-2091

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