Binding of Folic Acid Induces Specific Self-Aggregation of Lactoferrin : Thermodynamic Characterization
In the study presented here, we investigated the interaction at pH 5.5 between folic acid (FA) and lactoferrin (LF), a positively charged protein. We found a binding constant Ka of 10(5) M(-1) and a high stoichiometry of 10 mol of FA/mol of LF. The size and charge of the complexes formed evolved dur...
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Détails bibliographiques
Publié dans: | Langmuir : the ACS journal of surfaces and colloids. - 1985. - 31(2015), 45 vom: 17. Nov., Seite 12481-8
|
Auteur principal: |
Tavares, Guilherme M
(Auteur) |
Autres auteurs: |
Croguennec, Thomas,
Lê, Sébastien,
Lerideau, Olivia,
Hamon, Pascaline,
Carvalho, Antônio F,
Bouhallab, Saïd |
Format: | Article en ligne
|
Langue: | English |
Publié: |
2015
|
Accès à la collection: | Langmuir : the ACS journal of surfaces and colloids
|
Sujets: | Journal Article
Research Support, Non-U.S. Gov't
LTF protein, human
Protein Aggregates
Folic Acid
935E97BOY8
Lactoferrin
EC 3.4.21.- |