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Volumn 49, Issue 5, 2001, Pages 2609-2618

Interaction of β-lactoglobulin with small hydrophobic ligands as monitored by fluorometry and equilibrium dialysis: Nonlinear quenching effects related to protein - Protein association

Author keywords

Lactoglobulin; Binding parameters; Equilibrium dialysis; Flavor compounds; Fluorescence spectroscopy; Hydrophobic and steric effects

Indexed keywords

BETA IONONE; BETA LACTOGLOBULIN; LACTOGLOBULIN; LACTONE DERIVATIVE; LIGAND; PROTEIN; RETINOL;

EID: 0034849396     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf0012188     Document Type: Article
Times cited : (86)

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  • 6
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  • 7
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    • Fluorimetric analysis of interactions between β-lactoglobulin and flavor compounds
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    • Muresan, S.; Leguijt, T. Fluorimetric analysis of interactions between β-lactoglobulin and flavor compounds. In COST96: Interaction of Food Matrix with Small Ligands Influencing Flavor and Texture; Zacharoff, A. B., Ed.; European Commission: Luxembourg, 1997; Vol. 2, pp 45-51.
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  • 8
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    • Interaction between β-lactoglobulin and aroma compounds: A review of the COST action
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    • Langourieux, S.; Escher, F. Interaction between β-lactoglobulin and aroma compounds: a review of the COST action. In COST96: Interaction of Food Matrix with Small Ligands Influencing Flavor and Texture; Escher, F., Ed.; European Commission: Luxembourg, 1999; Vol. 5, pp 81-96.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.