Characterization of the covalent binding of allyl isothiocyanate toβ-lactoglobulin by fluorescence quenching, equilibrium measurement, and mass spectrometry-Reference-Cited by-同舟云学术

Characterization of the covalent binding of allyl isothiocyanate toβ-lactoglobulin by fluorescence quenching, equilibrium measurement, and mass spectrometry

Published:2013-06-28 Issue:7 Volume:32 Page:1103-1117
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Keppler Julia Katharina,Koudelka Tomas,Palani Kalpana,Stuhldreier Mayra Christina,Temps Friedrich,Tholey Andreas,Schwarz Karin

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

http://www.tandfonline.com/doi/pdf/10.1080/10256018808623883

Reference73 articles.

1. Sub-Structures Formed in the Excited State are Responsible for Tryptophan Residues Fluorescence in β-Lactoglobulin

2. Protein stability function relations: β-lactoglobulin-A sulphydryl group reactivity and its relationship to protein unfolding stability

3. Interaction of bovine -lactalbumin with fatty acids as determined by partition equilibrium and fluorescence spectroscopy

4. In Vitro Digestion of β-Lactoglobulin Fibrils Formed by Heat Treatment at Low pH

5. Locating the binding sites of retinol and retinoic acid with milk β-lactoglobulin

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