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Table 2 Dissociation of BTN and its oxidized forms from BBP-A and AVD. Fluorescence spectroscopy and radiobiotin dissociation analysis data at 40°C are shown. Binding enthalpies were measured by ITC at 25°C. bBBP-A and commercial chicken AVD was used in the analyses.

From: Structure and characterization of a novel chicken biotin-binding protein A (BBP-A)

Ligand

kdiss × 10-4 s-1

Enthalpy (kcal/mol) (ITC)

Tm (°C) (DSC)

 

BBP-A

AVD

BBP-A

AVD

BBP-A

BSO

1.3a

-29.3 ± 0.1

-25.9 ± 0.1

116.9 ± 0.2

100.4 ± 0.2

D-biotin sulfone

3.3a

-25.1 ± 0.1

-21.4 ± 0.1

117.0 ± 0.0

101.4 ± 0.2

BTN

5.4b (4.4c)

-22.6 ± 0.1

-20.5 ± 0.1

117.0 ± 0.7

103.4 ± 0.1

  1. aFrom fluorescence spectroscopic analysis, excess of BTN was used as a competitive ligand.
  2. bFrom fluorescence spectroscopic analysis, excess of BSO was used as a competitive ligand.
  3. cValue obtained from [3H]-biotin dissociation analysis, excess of BTN was used as a competitive ligand.
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BMC Structural Biology

ISSN: 1472-6807

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