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- W213329114 abstract "Studies have been carried out on E-lg/pectin system, but none has provided a complete analysis of the inherent thermodynamic parameters. The aim of this work was to determine, at pH 4 and at 25°C, the binding constant, stoichiometry, enthalpy and entropy values for low- and high-methylated pectin (LM- and HM-pectin)/E-lg systems using isothermal titration calorimetry (ITC). The binding isotherms showed the occurrence of 2 types of binding sites on the pectin. The binding constants of the first binding site were 2,78x10 7 and 1,38x10 7 M -1 for the LMand HM-pectin/E-lg complexes, respectively. This site corresponds to the layer of E-lg molecules complexed on the immediate vicinity of a pectin molecule. The interaction with LM- and HM-pectin respectively released 15.2 and 10.0 kcal/mol of E-lg injected. The stoichiometry of the reaction was 7.0 and 5.7 E-lg molecules complexed on each LM- and HM-pectin molecule, respectively. The second binding site corresponds to the additional layers of E-lg molecules bonded by means of residual charges on E-lg/pectin complexes. The interaction on the second site had lower binding constants and released less heat. There were about 16.6 and 14.7 E-lg molecules complexed on the second site of LM- and HM-pectin, respectively." @default.
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- W213329114 date "2003-01-01" @default.
- W213329114 modified "2023-09-27" @default.
- W213329114 title "THERMODYNAMIC PARAMETERS OF E-LACTOGLOBULIN/PECTIN COMPLEXES DETERMINED BY ISOTHERMAL TITRATION CALORIMETRY" @default.
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