Pressure-induced denaturation of monomer β-lactoglobulin is partially irreversible: Comparison of monomer form (highly acidic pH) with dimer form (neutral pH)

Journal of Agricultural and Food Chemistry

Volumn 49, Issue 8, 2001, Pages 4052-4059

  Ikeuchi, Y ^a   Nakagawa, K ^b   Endo, T ^b   Suzuki, A ^b   Hayashi, T ^a   Ito, T ^a  

^a KYUSHU UNIVERSITY   (Japan)

^b NIIGATA UNIVERSITY   (Japan)

Author keywords

Lactoglobulin; Denaturation of protein; High pressure; Hydrogen deuterium exchange; NMR

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; BETA LACTOGLOBULIN; DIMER; LACTOGLOBULIN; MONOMER; PARINARIC ACID; RETINOL; TRYPTOPHAN;

ACIDITY; ARTICLE; CHEMISTRY; CIRCULAR DICHROISM; COMPARATIVE STUDY; FLUORESCENCE SPECTROSCOPY; HYDROSTATIC PRESSURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRESSURE; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SPECTROFLUOROMETRY;

CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; LACTOGLOBULINS; MAGNETIC RESONANCE SPECTROSCOPY; PRESSURE; PROTEIN DENATURATION; SPECTROMETRY, FLUORESCENCE;

EID: 0034850884     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf001364d     Document Type: Article

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