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Volumn 277, Issue 43, 2002, Pages 40717-40721
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Thermal unfolding of soybean peroxidase: Appropriate high denaturant concentrations induce cooperativity allowing the correct measurement of thermodynamic parameters
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Author keywords
[No Author keywords available]
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Indexed keywords
CONCENTRATION (PROCESS);
ENZYMES;
PLANTS (BOTANY);
SEED;
THERMODYNAMICS;
HEAT-INDUCED DENATURATION;
THERMAL UNFOLDING MECHANISM;
BIOCHEMISTRY;
GUANIDINE;
HEME;
PEROXIDASE;
ARTICLE;
CIRCULAR DICHROISM;
DENATURATION;
ENZYME MECHANISM;
PRIORITY JOURNAL;
PROTEIN FOLDING;
SEED HUSK;
SOYBEAN;
TEMPERATURE DEPENDENCE;
THERMODYNAMICS;
CIRCULAR DICHROISM;
HEAT;
PEROXIDASES;
PROTEIN DENATURATION;
SOYBEANS;
SPECTROPHOTOMETRY, ULTRAVIOLET;
THERMODYNAMICS;
GLYCINE MAX;
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EID: 0037174849
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M208129200 Document Type: Article |
Times cited : (25)
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References (32)
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