Research article
Investigation of the chaperone function of the small heat shock protein — AgsA
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* Corresponding author: Toshifumi Tomoyasu tomoyasu@bio.tokushima-u.ac.jp
Department of Biological Science and Technology, Institute of Technology and Science, The University of Tokushima Graduate School, Minami-josanjima-cho, Tokushima 770-8506, Japan
BMC Biochemistry 2010, 11:27 doi:10.1186/1471-2091-11-27
Published: 24 July 2010Additional files
Additional file 1:
Table S1. Percentage of turbidity of DTT-denatured lysozyme.
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Additional file 2:
Table S2. Percentage of turbidity of DTT-denatured insulin.
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Additional file 3:
Table S3. Percentage of turbidity of heat-denatured MDH.
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Table S4. Percentage of turbidity of heat-denaturfed CS.
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Additional file 5:
Table S5. Cooperative effect of AgsA and ΔC11 on the aggregation prevention of several substrates.
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Additional file 6:
Figure S1. Measurement of subunit exchange between AgsA and IbpB.
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