Pressure denaturation and aggregation of β-lactoglobulin studied by intrinsic fluorescence depolarization, Rayleigh scattering, radiationless energy transfer and hydrophobic fluoroprobing

Journal of Dairy Research

Volumn 66, Issue 4, 1999, Pages 545-558

  Stapelfeldt, Henrik ^a,b   Skibsted, Leif H ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b DANISH VETERINARY AND FOOD ADMINISTRATION   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AQUEOUS SOLUTION; BETA LACTOGLOBULIN; DIFFUSION; ENERGY TRANSFER; FLUORESCENCE; HYDROPHOBICITY; IONIC STRENGTH; MODEL; PARINARIC ACID; PRESSURE; PROBE; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN COMPLEX; PROTEIN DENATURATION; PROTEIN FOLDING; RAYLEIGH SCATTERING; SOLVENT; STOICHIOMETRY; TEMPERATURE;

ANILINO NAPHTHALENESULFONATES; CHEMISTRY, PHYSICAL; ENERGY TRANSFER; FATTY ACIDS, UNSATURATED; FLUORESCENCE POLARIZATION; FLUORESCENT DYES; LACTOGLOBULINS; OSMOLAR CONCENTRATION; PRESSURE; PROTEIN DENATURATION; SCATTERING, RADIATION; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; UREA;

EID: 0033231061     PISSN: 00220299     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0022029999003714     Document Type: Article

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